SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_043766493.1 NCBI__GCF_000733765.1:WP_043766493.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

E4PMA5 Glucosylglycerol phosphorylase; GGoP; 2-O-alpha-D-glucopyranosylglycerol:phosphate alpha-D-glucosyltransferase; 2-O-alpha-D-glucosylglycerol phosphorylase (retaining); EC 2.4.1.359 from Marinobacter adhaerens (strain DSM 23420 / HP15) (see paper)
68% identity, 99% coverage: 1:474/480 of query aligns to 1:474/480 of E4PMA5

query
sites
E4PMA5

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Y194 (= Y194) mutation to A: 2.7% of wild-type catalytic activity.
A333 (= A333) mutation to D: 0.3% of wild-type catalytic activity. Does not gain activity on sucrose.
Q336 (= Q336) mutation to A: 2.6% of wild-type catalytic activity.

7xdqA Crystal structure of a glucosylglycerol phosphorylase mutant from marinobacter adhaerens
67% identity, 98% coverage: 3:474/480 of query aligns to 1:464/470 of 7xdqA

query
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7xdqA

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binding beta-D-glucopyranose: D47 (= D49), F50 (= F52), H85 (= H87), R186 (= R188), E229 (= E231), D287 (= D289)

D9TT09 Sucrose 6(F)-phosphate phosphorylase; Sucrose 6'-phosphate phosphorylase; SPP; EC 2.4.1.329 from Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium thermosaccharolyticum) (see 2 papers)
41% identity, 98% coverage: 1:470/480 of query aligns to 1:479/488 of D9TT09

query
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D9TT09

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D

S

A

A

L

L

K

N

Q

C

N

D

D

D

A

A

Y

Y

I

L

A

A

R

R

A

A

I

I

Q

Q

L

F

F

F

A

T

P

P

G

G

I

I

P

P

Q

Q

I

V

Y

Y

V

V

G

G

L

L

A

A

G

G

T

V

N

N

D

D

E

F

E

E

L

A

M

V

E

K

H

K

T

T

G

K

E

E

L

G

R

R

D

E

I

I

N

N

R

R

T

H

Y

N

F

Y

D

G

L

L

E

K

A

E

V

I

A

E

E

E

A

S

T

V

E

Q

K

K

P

N

V

V

R

Q

R

R

L

L

I

L

Q

K

L

L

L

I

E

R

F

F

R

R

C

N

S

E

H

Y

P

E

A

A

F

F

R

N

G

G

T

E

F

F

E

F

L

I

V

E

Y

D

S

C

N

R

D

K

T

D

S

E

V

I

S

R

M

L

Q

T

W

W

K

K

N

K

G

D

D

D

A

K

K

R

A

C

L

S

L

L

F

F

V

I

D

D

L

L

N

K

F

T

K

Y

K

K

T

T

V

I

R

D

Y

Y

R

I

D

N

E

E

R134 (= R131) mutation to A: Shows a decreased ratio of activity on phosphorylated fructose over fructose. Displays increased transglycosylation activity on a broad range of bulky acceptors.
R135 (≠ K132) mutation to A: Displays similar activity as the wild-type.
K301 (vs. gap) mutation to A: Displays similar activity as the wild-type.
H344 (≠ Y335) mutation to Y: Shows a decreased ratio of activity on phosphorylated fructose over fructose.

P10249 Sucrose phosphorylase; Glucosyltransferase-A; GTF-A; Sucrose glucosyltransferase; EC 2.4.1.7 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see paper)
38% identity, 97% coverage: 1:466/480 of query aligns to 1:470/481 of P10249

query
sites
P10249

M
|
M

I

P

L

I

R

I

N

N

L

K

P

T

H

M

L

L

I

I

A

T

Y

Y

P

A

D

D

R

S

M

L

G

G

S

K

S

N

I

L

S

K

D

E

L

L

H

N

K

E

V

N

M

I

R

E

E

N

H

Y

F

F

P

G

R

D

C

A

F

V

G

G

V

V

H

H

L

L

P

P

P

F

F

F

P

P

S

S

N

T

A

G

D

D

G

R

G

G

F

F

S

A

P

P

L

I

T

D

H

Y

R

H

E

E

I

V

D

D

P

S

R

A

Y

F

G

G

S

D

W

W

E

D

V

V

E

K

A

C

L

L

A

G

A

E

E

K

Y

Y

D

Y

L

L

C

M

L

F

D

D

L

F

V

M

L

I

N

N

H

H

I

I

A

S

D

R

E

Q

S

S

P

K

E

Y

F

Y

K

K

D

D

F

Y

L

Q

A

E

N

K

G

H

R

E

D

A

S

S

R

A

Y

Y

A

K

E

D

L

L

F

F

V

L

D

N

V

W

D

D

A

K

L

F

-

W

-

P

-

K

G

N

E

R

I

P

T

T

S

Q

D

E

D

D

L

V

A

D

K

L

I

I

H

Y

I

K

R

R

K

K

E

D

K

R

E

A

P

P

F

K

R

Q

E

E

V

I

T

Q

L

F

A

A

N

D

G

G

E

S

K

V

K

E

R

H

V

L

W

W

C

N

T

T

F

F

T

G

E

E

K

E

Q

Q

V

I

D

D

L

L

N

D

Y

V

D

T

A

K

E

E

A

V

T

T

Y

M

D

D

F

F

M

I

E

R

E

S

N

T

L

I

R

E

V

N

M

L

T

A

G

A

H

N

G

G

V

C

K

D

L

L

F

I

R

R

L

L

D

D

A

A

F

F

G

A

Y

Y

T

A

T

V

K

K

I

L

G

D

T

T

S

N

C

D

F

F

L

F

V

V

E

E

P

P

D

E

V

I

Y

W

D

T

I

L

L

L

G

D

W

K

F

V

H

R

R

D

T

I

A

A

N

A

R

V

M

S

G

G

A

A

E

E

V

I

L

L

P

P

E

E

V

I

H

H

D

E

H

H

S

Y

S

T

Y

I

Q

Q

F

F

A

K

I

I

G

A

M

D

R

H

G

D

M

Y

R

Y

P

V

Y

Y

G

D

F

F

A

A

L

L

P

P

P

M

L

V

L

T

L

L

Y

Y

S

S

L

L

L

Y

D

S

A

S

N

K

S

V

V

D

H

R

L

L

K

A

N

K

W

W

L

L

R

K

V

M

C

S

P

P

R

M

N

K

Q

Q

I

F

T

T

V

T

L

L

D

D

T

T

H

H

D

D

G

G

I

I

C

G

I

V

P

V

D

D

V

V

E

K

G

D

I

I

L

L

P

T

A

D

D

E

K

E

I

I

Q

T

A

Y

V

T

I

S

D

N

N

E

V

L

S

Y

Q

K

R

V

S

G

A

A

D

N

P

V

I

N

L

R

R

K

R

Y

S

S

A

T

A

A

N

E

V

Y

H

N

S

N

V

L

G

D

A

-

I

I

Y

Y

Q

Q

L

I

T

N

C

S

T

T

F

Y

Y

Y

D

S

A

A

L

L

K

G

Q

D

N

D

D

D

D

Q

A

K

Y

Y

I

F

A

L

A

A

R

R

A

L

I

I

Q

Q

L

A

F

F

A

A

P

P

G

G

I

I

P

P

Q

Q

I

V

Y

Y

V

V

G

G

L

F

L

L

A

A

G

G

T

K

N

N

D

D

E

L

E

E

L

L

M

L

E

E

H

S

T

T

G

K

E

E

L

G

R

R

D

N

I

I

N

N

R

R

T

H

Y

Y

F

Y

D

S

L

S

E

E

A

E

V

I

A

A

E

K

A

E

T

V

E

K

K

R

P

P

V

V

R

K

R

A

L

L

I

L

Q

N

L

L

L

F

E

T

F

Y

R

R

C

N

S

Q

H

S

P

A

A

A

F

F

-

D

-

L

R

D

G

G

T

R

F

I

E

E

L

V

V

E

Y

T

S

P

N

N

D

E

T

A

S

T

V

I

S

V

M

I

Q

E

W

R

K

Q

N

N

G

K

D

D

A

G

K

S

A

H

L

I

L

A

F

K

V

A

D

E

L
x
I

N
|
N

F
x
L

K
x
Q

K
x
D

T
x
M

T
|
T

V
x
Y

R
|
R

M1 (= M1) modified: Initiator methionine, Removed

Sites not aligning to the query:

462:481 mutation Missing: Loss of glucan synthesis.

7znpA Structure of amedsp
38% identity, 98% coverage: 3:472/480 of query aligns to 2:489/502 of 7znpA

query
sites
7znpA

L

I

R

R

N

N

L

G

P

V

H

Q

L

L

I

I

A

T

Y

Y

P

A

D

D

R

R

M

L

G

G

-

D

S

G

S

N

I

I

S

E

D

S

L

L

H

T

K

N

V

L

M

L

R

D

E

G

H

P

F

L

P

K

R

G

C

L

F

F

G

K

G

G

V

V

H

H

L

I

L

L

P

P

-

F

P

Y

F

Y

P

P

S

Y

N

D

A

G

-

E

D

D

G

A

G

G

F

F

S

D

P

P

L

I

T

D

H

H

R

T

E

T

I

V

D

D

P

E

R

R

Y

L

G

G

S

D

W

W

E

N

V

I

E

K

A

K

L

L

A
x
G

A

E

E

S

Y
x
V

D

D

L

I

C

M

L

A

D

D

L

L

V

I

L

V

N

N

H

H

I

M

A

S

D

G

E

Q

S

S

P

E

E

A

F

F

K

T

D

D

F

V

L

L

A

K

N

K

G

G

R

R

D

E

S

S

R

E

Y

Y

A

W

E

P

L

L

F

F

V

L

D

T

V

K

D

E

A

D

L

V

G

-

E

-

I

F

T

S

S

G

D

N

D

D

L

Q

A

A

K

E

I

I

H

D

-

E

-

Q

-

I

-

A

-

K

-

V

I

F

R

R

K

P

E

R

K

P

E

T

P

P

F

F

-

F

-

S

-

D

R

Y

E

E

V

V

T

G

L

I

A

E

N

T

G

D

E

S

K

T

K

E

R

T

V

V

-

P

-

F

W

W

C

T

T

T

F

F

T

T

E

S

K

N

Q

Q

V

I

D

D

L

I

N

D

Y

V

D

E

A

S

E

E

A

L

T

G

Y

K

D

E

F

Y

M

L

E

S

N

I

L

L

R

Q

V

S

M

F

T

T

G

E

H

S

G
x
N

V

V

K
x
D

L

L

F

I

R

R

L

L

D

D

A

A

F

A

G

G

Y

Y

T

A

T

I

K

K

K

R

I

A

G

G

T

S

S

N

C

C

F

F

L

M

V

L

E

E

P

-

D

E

V

T

Y

F

D

E

I

F

L

I

G

E

W

A

F

L

H

S

R

K

T

R

A

A

N

R

R

T

M

M

G

G

A

M

E

Q

V

C

L

L

P

V

E

E

V

I

H

H

D

S

H

H

S

Y

S

Q

Y

T

Q

Q

F

I

A

D

I

I

G

A

M

A

R

R

G

C

M

D

R

S

P

V

Y

Y

G

D

F

F

A

A

L

L

P

P

L

L

L

V

L

L

Y

H

S

T

L

L

L

F

D

T

A

K

N

D

S

A

V

S

H

A

L

L

K

A

N

H

W

W

L

L

R

S

V

I

C

S

P

P

R

R

N

N

Q

C

I

F

T

T

V

V

L

L

D

D

T

T

H

H

D

D

G

G

I

I

C

G

I

I

P

V

D

D

V

V

-

G

-

A

-

S

-

G

-

D

-

K

E

P

G

G

I

L

L

I

P

S

A

A

D

D

K

A

I

I

Q

N

A

A

V

L

I

V

D

E

N

Q

V

I

S

H

Q

V

R

N

S

S

A

N

D

G

P

E

I

S

L

K

R

K

R

A

S

T

A

G

A

A

N

A

V

A

H

N

S

N

V

V

G

D

A

-

I

L

Y

Y

Q

Q

L

V

T

N

C

C

T

T

F

Y

Y

Y

D

D

A

A

L

L

K

G

Q

K

N

D

D

D

D

F

A

A

Y

Y

I

L

A

V

A

A

R

R

A

A

I

I

Q

Q

L

F

F

F

A

S

P

P

G

G

I

I

P

P

Q

Q

I

V

Y

Y

V

G

G

G

L

L

A

A

G

A

T

H

N

N

D

D

E

M

E

E

L

L

M

L

E

A

H

N

T

T

G

N

E

V

L

G

R

R

D

D

I

I

N

N

R

R

T

P

Y

Y

F

L

D

T

L

T

E

A

A

M

V

V

A

E

E

D

A

A

T

I

E

Q

K

K

P

P

V

V

R

K

R

G

L

L

I

M

Q

Q

L

L

L

I

E

T

F

L

R

R

C

N

S

E

H

N

P

K

A

A

F

F

R

G

G

G

T

A

F

F

E

D

L

V

V

T

Y

Y

S

T

N

D

D

N

T

T

S

L

V

V

S

-

M

L

Q

S

W

W

K

S

N

N

-

D

G

G

D

D

A

A

K

A

A

S

L

L

L

T

-

V

-

D

F

F

V

A

D

A

L

M

N

D

F

A

K

T

K

I

T

N

T

T

V

V

R

S

Y

N

R

G

D

E

E

E

R

S

T

T

binding magnesium ion: G76 (≠ A74), V79 (≠ Y77), N194 (≠ G183), D196 (≠ K185)

A0ZZH6 Sucrose phosphorylase; SP; SPase; EC 2.4.1.7 from Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) (see paper)
36% identity, 94% coverage: 3:454/480 of query aligns to 1:463/504 of A0ZZH6

query
sites
A0ZZH6

L

M

R

K

N

N

L

K

P

V

H

Q

L

L

I

I

A

T

Y

Y

P

A

D

D

R

R

M

L

G

G

-

D

S

G

S

T

I

I

S

K

D

S

L

M

H

T

K

D

V

I

M

L

R

R

E

T

H

R

F

F

P

D

R

G

C

V

F

Y

G

D

G

G

V

V

H

H

L

I

L

L

P

P

P

F

F

F

P

T

-

P

-

F

S

D

N

G

A

A

D
|
D

G

A

G

G

F

F

S

D

P

P

L

I

T

D

H

H

R

T

E

K

I

V

D

D

P

E

R

R

Y

L

G

G

S

S

W

W

E

D

V

V

E

A

A

E

L

L

A

S

A

K

E

T

Y

H

D

N

L

I

C

M

L

V

D

D

L

A

V

I

L

V

N

N

H
|
H

I

M

A

S

D

W

E

E

S

S

P

K

E

Q

F

F

K

Q

D

D

F

V

L

L

A

A

N

K

G

G

R

E

D

E

S

S

R

E

Y

Y

A

Y

E

P

L

M

F

F

V

L

D

T

V

M

D

S

A

S

L

V

-

F

-

P

G

N

E

G

I

A

T

T

S

E

D

E

D

D

L

L

A

A

K

G

I

I

H

Y

I

R

R

P

K

R

E

P

K

G

E

L

P

P

F

F

R

T

E

H

V

Y

T

K

L

F

A

A

N

-

G

G

E

K

K

T

K

R

R

L

V

V

W

W

C

V

T

S

F

F

T

T

E

P

K

Q

Q

Q

V

V

D

D

L

I

N

D

Y

T

D

D

A

S

E

D

A

K

T

G

Y

W

D

E

F

Y

M

L

E

M

E

S

N

I

L

F

R

D

V

Q

M

M

T

A

G

A

H

S

G

H

V

V

K

S

L

Y

F

I

R
|
R

L
|
L

D
|
D

A

A

F

V

G

G

Y

Y

T

G

T

A

K

K

K

E

I

A

G

G

T

T

S

S

C

C

F

F

L

M

V

T

E

-

P

P

D

K

V

T

Y

F

D

K

I

L

L

I

G

S

W

R

F

L

H

R

R

E

T

E

A

G

N

V

R

K

M

R

G

G

A

L

E

E

V

I

L

L

P

I

E
|
E

V

V

H

H

D

S

H

Y

S

Y

S

K

Y

K

Q

Q

F

V

A

E

I

I

G

A

M

S

R

K

G

V

M

D

R

R

P

V

Y

Y

G

D

F

F

A

A

L

L

P

P

L

L

Y

H

S

A

L

L

L

S

D

T

A

G

N

H

S

V

V

E

H

P

L

V

K

A

N

H

W

W

L

T

R

D

V

I

C

R

P

P

R

N

N

N

Q

A

I

V

T

T

V

V

L

L

D

D

T

T

H
|
H

D
|
D

G

G

I

I

C

G

I

V

P

I

D

D

V

I

-

G

-

S

-

D

-

Q

-

L

-

D

-

R

-

S

-

L

E

K

G

G

I

L

L

V

P

P

A

D

D

E

K

D

I

V

Q

D

A

N

V

L

I

V

D

N

N

T

V

I

S

H

Q

A

R

N

S

T

A

H

D

G

P

E

I

S

L

Q

R

A

S

T

A

G

A

A

N

A

V

A

H

S

S

N

V

L

G
x
D

A

-

I
x
L

Y
|
Y

Q
|
Q

L

V

T

N

C

S

T

T

F

Y

Y

Y

D

S

A

A

L

L

K

G

Q

C

N

N

D

D

D

Q

A

H

Y

Y

I

I

A

A

R

R

A

A

I

V

Q

Q

L

F

F

F

A

L

P

P

G

G

I

V

P

P

Q

Q

I

V

Y

Y

V

V

G

G

L

A

L

L

A

A

G

G

T

K

N

N

D

D

E

M

E

E

L

L

M

L

E

R

H

K

T

T

G

N

E

N

L

G

R
|
R

D

D

I

I

N

N

R

R

T

H

Y

Y

F

Y

D

S

L

T

E

A

A

E

V

I

A

D

E

E

A

N

T

L

E

K

K

R

P

P

V

V

R

K

R

A

L

L

I

N

Q

A

L

L

L

A

E

K

F

F

R

R

C

N

S

E

H

L

P

D

A

A

F

F

R

D

G

G

T

T

F

F

E

S

L

Y

V

T

Y

T

S

D

N

D

D

D

T

T

S

S

V

I

S

S

M

F

Q

T

W

W

K

R

N

G

G

E

D

T

A

S

K

Q

A

A

L

T

L

L

D50 (= D49) binding substrate
H88 (= H87) binding sucrose
RLD 190:192 (= RLD 188:190) binding sucrose
D192 (= D190) active site, Nucleophile
E232 (= E231) binding sucrose; mutation to Q: Loss of catalytic activity.
HD 289:290 (= HD 288:289) binding sucrose
D-LYQ 342:345 (≠ GAIYQ 332:336) binding sucrose
Q345 (= Q336) mutation to F: Decreases affinity for sucrose. Highly improves in vitro activity towards aromatic acceptors, allowing efficient glucosylation of resveratrol, (+)-catechin and (-)-epicatechin.
R399 (= R390) binding sucrose

2gduA E232q mutant of sucrose phosphorylase from bifidobacterium adolescentis in complex with sucrose (see paper)
36% identity, 94% coverage: 3:454/480 of query aligns to 1:463/504 of 2gduA

query
sites
2gduA

L

M

R

K

N

N

L

K

P

V

H

Q

L

L

I

I

A

T

Y

Y

P

A

D

D

R

R

M

L

G

G

-

D

S

G

S

T

I

I

S

K

D

S

L

M

H

T

K

D

V

I

M

L

R

R

E

T

H

R

F

F

P

D

R

G

C

V

F

Y

G

D

G

G

V

V

H

H

L

I

L

L

P

P

P

F

F

F

P

T

-

P

-

F

S

D

N

G

A

A

D
|
D

G

A

G

G

F
|
F

S

D

P

P

L

I

T

D

H

H

R

T

E

K

I

V

D

D

P

E

R

R

Y

L

G

G

S

S

W

W

E

D

V

V

E

A

A

E

L

L

A

S

A

K

E

T

Y

H

D

N

L

I

C

M

L

V

D

D

L

A

V

I

L

V

N

N

H
|
H

I

M

A

S

D

W

E

E

S

S

P

K

E

Q

F

F

K

Q

D

D

F

V

L

L

A

A

N

K

G

G

R

E

D

E

S

S

R

E

Y

Y

A

Y

E

P

L

M

F

F

V

L

D

T

V

M

D

S

A

S

L

V

-

F

-

P

G

N

E

G

I

A

T

T

S

E

D

E

D

D

L

L

A

A

K

G

I

I

H

Y

I

R

R

P

K

R

E

P

K

G

E

L

P

P

F

F

R

T

E

H

V

Y

T

K

L

F

A

A

N

-

G

G

E

K

K

T

K

R

R

L

V

V

W

W

C

V

T

S

F
|
F

T

T

E

P

K

Q

Q

Q

V

V

D

D

L

I

N

D

Y

T

D

D

A

S

E

D

A

K

T

G

Y

W

D

E

F

Y

M

L

E

M

E

S

N

I

L

F

R

D

V

Q

M

M

T

A

G

A

H

S

G

H

V

V

K

S

L

Y

F

I

R

R

L

L

D
|
D

A
|
A

F

V

G

G

Y

Y

T

G

T

A

K

K

K

E

I

A

G

G

T

T

S

S

C

C

F

F

L

M

V

T

E

-

P

P

D

K

V

T

Y

F

D

K

I

L

L

I

G

S

W

R

F

L

H

R

R

E

T

E

A

G

N

V

R

K

M

R

G

G

A

L

E

E

V

I

L

L

P

I

E
x
Q

V

V

H
|
H

D

S

H

Y

S

Y

S

K

Y

K

Q

Q

F

V

A

E

I

I

G

A

M

S

R

K

G

V

M

D

R

R

P

V

Y

Y

G

D

F

F

A

A

L

L

P

P

L

L

Y

H

S

A

L

L

L

S

D

T

A

G

N

H

S

V

V

E

H

P

L

V

K

A

N

H

W

W

L

T

R

D

V

I

C

R

P

P

R

N

N

N

Q

A

I

V

T

T

V

V

L

L

D

D

T

T

H
|
H

D
|
D

G

G

I

I

C

G

I

V

P

I

D

D

V

I

-

G

-

S

-

D

-

Q

-

L

-

D

-

R

-

S

-

L

E

K

G

G

I

L

L

V

P

P

A

D

D

E

K

D

I

V

Q

D

A

N

V

L

I

V

D

N

N

T

V

I

S

H

Q

A

R

N

S

T

A

H

D

G

P

E

I

S

L

Q

R

A

S

T

A

G

A

A

N

A

V

A

H

S

S

N

V

L

G
x
D

A

-

I

L

Y

Y

Q
|
Q

L

V

T

N

C

S

T

T

F

Y

Y

Y

D

S

A

A

L

L

K

G

Q

C

N

N

D

D

D

Q

A

H

Y

Y

I

I

A

A

R

R

A

A

I

V

Q

Q

L

F

F

F

A

L

P

P

G

G

I

V

P

P

Q

Q

I

V

Y

Y

V

V

G

G

L

A

L

L

A

A

G

G

T

K

N

N

D

D

E

M

E

E

L

L

M

L

E

R

H

K

T

T

G

N

E

N

L

G

R
|
R

D

D

I

I

N

N

R

R

T

H

Y

Y

F

Y

D

S

L

T

E

A

A

E

V

I

A

D

E

E

A

N

T

L

E

K

K

R

P

P

V

V

R

K

R

A

L

L

I

N

Q

A

L

L

L

A

E

K

F

F

R

R

C

N

S

E

H

L

P

D

A

A

F

F

R

D

G

G

T

T

F

F

E

S

L

Y

V

T

Y

T

S

D

N

D

D

D

T

T

S

S

V

I

S

S

M

F

Q

T

W

W

K

R

N

G

G

E

D

T

A

S

K

Q

A

A

L

T

L

L

binding beta-D-fructofuranose: F156 (= F154), A193 (= A191), Q232 (≠ E231), H234 (= H233), D290 (= D289), D342 (≠ G332), Q345 (= Q336), R399 (= R390)
binding alpha-D-glucopyranose: D50 (= D49), F53 (= F52), H88 (= H87), F156 (= F154), D192 (= D190), Q232 (≠ E231), H289 (= H288), D290 (= D289), R399 (= R390)

5c8bB Structural insights into the redesign of a sucrose phosphorylase by induced loop repositioning (see paper)
36% identity, 94% coverage: 3:454/480 of query aligns to 1:463/504 of 5c8bB

query
sites
5c8bB

L

M

R

K

N

N

L

K

P

V

H

Q

L

L

I

I

A

T

Y

Y

P

A

D

D

R

R

M

L

G

G

-

D

S

G

S

T

I

I

S

K

D

S

L

M

H

T

K

D

V

I

M

L

R

R

E

T

H

R

F

F

P

D

R

G

C

V

F

Y

G

D

G

G

V

V

H

H

L

I

L

L

P

P

P

F

F

F

P

T

-

P

-

F

S

D

N

G

A

A

D
|
D

G

A

G

G

F

F

S

D

P

P

L

I

T

D

H

H

R

T

E

K

I

V

D

D

P

E

R

R

Y

L

G

G

S

S

W

W

E

D

V

V

E

A

A

E

L

L

A

S

A

K

E

T

Y

H

D

N

L

I

C

M

L

V

D

D

L

A

V

I

L

V

N

N

H

H

I

M

A

S

D

W

E

E

S

S

P

K

E

Q

F

F

K

Q

D

D

F

V

L

L

A

A

N

K

G

G

R

E

D

E

S

S

R

E

Y

Y

A

Y

E

P

L

M

F

F

V

L

D

T

V

M

D

S

A

S

L

V

-

F

-

P

G

N

E

G

I

A

T

T

S

E

D

E

D

D

L

L

A

A

K

G

I

I

H

Y

I

R

R

P

K

R

E

P

K

G

E

L

P

P

F

F

R

T

E

H

V

Y

T

K

L

F

A

A

N

-

G

G

E

K

K

T

K

R

R

L

V

V

W

W

C

V

T

S

F

F

T

T

E

P

K

Q

Q

Q

V

V

D

D

L

I

N

D

Y

T

D

D

A

S

E

D

A

K

T

G

Y

W

D

E

F

Y

M

L

E

M

E

S

N

I

L

F

R

D

V

Q

M

M

T

A

G

A

H

S

G

H

V

V

K

S

L

Y

F

I

R

R

L

L

D

D

A

A

F

V

G

G

Y

Y

T

G

T

A

K

K

K

E

I

A

G

G

T

T

S

S

C

C

F

F

L

M

V

T

E

-

P

P

D

K

V

T

Y

F

D

K

I

L

L

I

G

S

W

R

F

L

H

R

R

E

T

E

A

G

N

V

R

K

M

R

G

G

A

L

E

E

V

I

L

L

P

I

E
|
E

V

V

H

H

D

S

H

Y

S

Y

S

K

Y

K

Q

Q

F

V

A

E

I

I

G

A

M

S

R

K

G

V

M

D

R

R

P

V

Y

Y

G

D

F

F

A

A

L

L

P

P

L

L

Y

H

S

A

L

L

L

S

D

T

A

G

N

H

S

V

V

E

H

P

L

V

K

A

N

H

W

W

L

T

R

D

V

I

C

R

P

P

R

N

N

N

Q

A

I

V

T

T

V

V

L

L

D

D

T

T

H

H

D
|
D

G

G

I

I

C

G

I

V

P

I

D

D

V

I

-

G

-

S

-

D

-

Q

-

L

-

D

-

R

-

S

-

L

E

K

G

G

I

L

L

V

P

P

A

D

D

E

K

D

I

V

Q

D

A

N

V

L

I

V

D

N

N

T

V

I

S

H

Q

A

R

N

S

T

A

H

D

G

P

E

I

S

L

Q

R

A

S

T

A

G

A

A

N

A

V

A

H

S

S

N

V

L

G

D

A

-

I

L

Y

Y

Q

F

L

V

T

N

C

S

T

T

F

Y

Y

Y

D

S

A

A

L

L

K

G

Q

C

N

N

D

D

D

Q

A

H

Y

Y

I

I

A

A

R

R

A

A

I

V

Q

Q

L

F

F

F

A

L

P

P

G

G

I

V

P

P

Q

Q

I

V

Y

Y

V

V

G

G

L

A

L

L

A

A

G

G

T

K

N

N

D

D

E

M

E

E

L

L

M

L

E

R

H

K

T

T

G

N

E

N

L

G

R

R

D

D

I

I

N

N

R

R

T

H

Y

Y

F

Y

D

S

L

T

E

A

A

E

V

I

A

D

E

E

A

N

T

L

E

K

K

R

P

P

V

V

R

K

R

A

L

L

I

N

Q

A

L

L

L

A

E

K

F

F

R

R

C

N

S

E

H

L

P

D

A

A

F

F

R

D

G

G

T

T

F

F

E

S

L

Y

V

T

Y

T

S

D

N

D

D

D

T

T

S

S

V

I

S

S

M

F

Q

T

W

W

K

R

N

G

G

E

D

T

A

S

K

Q

A

A

L

T

L

L

binding beta-D-glucopyranose: D50 (= D49), E232 (= E231), D290 (= D289)

5m9xB Structure of sucrose phosphorylase from bifidobacterium adolescentis bound to glycosylated resveratrol (see paper)
35% identity, 94% coverage: 3:454/480 of query aligns to 1:463/504 of 5m9xB

query
sites
5m9xB

L

M

R

K

N

N

L

K

P

V

H

Q

L

L

I

I

A

T

Y

Y

P

A

D

D

R

R

M

L

G

G

-

D

S

G

S

T

I

I

S

K

D

S

L

M

H

T

K

D

V

I

M

L

R

R

E

T

H

R

F

F

P

D

R

G

C

V

F

Y

G

D

G

G

V

V

H

H

L

I

L

L

P

P

P

F

F

F

P

T

-

P

-

F

S

D

N

G

A

A

D
|
D

G

A

G

G

F
|
F

S

D

P

P

L

I

T

D

H

H

R

T

E

K

I

V

D

D

P

E

R

R

Y

L

G

G

S

S

W

W

E

D

V

V

E

A

A

E

L

L

A

S

A

K

E

T

Y

H

D

N

L

I

C

M

L

V

D

D

L

A

V

I

L

V

N

N

H

H

I

M

A

S

D

W

E

E

S

S

P

K

E

Q

F

F

K

Q

D

D

F

V

L

L

A

A

N

K

G

G

R

E

D

E

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S

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Y

Y

A

Y

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L

M

F

F

V

L

D

T

V

M

D

S

A

S

L

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-

F

-

P

G

N

E

G

I

A

T

T

S

E

D

E

D

D

L

L

A

A

K

G

I

I

H

Y

I

R

R
x
P

K
x
R

E

P

K

G

E

L

P

P

F

F

R

T

E

H

V

Y

T

K

L

F

A

A

N

-

G

G

E

K

K

T

K

R

R

L

V

V

W

W

C

V

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S

F

F

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T

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K

Q

Q

Q

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V

D

D

L

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L

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M

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M

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K

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L

Y

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I

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L

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x
N

A
|
A

F

V

G

G

Y

Y

T

G

T

A

K

K

K

E

I

A

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G

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T

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S

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C

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|
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H

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W

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P

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N

N

N

Q

A

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V

T

T

V

V

L

L

D

D

T

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H
|
H

D
|
D

G

G

I

I

C

G

I

V

P

I

D

D

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I

-

G

-

S

-

D

-

Q

-

L

-

D

-

R

-

S

-

L

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K

G

G

I

L

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D

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D

A

N

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L

I

V

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N

N

T

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I

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H

Q

A

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N

S

T

A

H

D

G

P

E

I

S

L

Q

R

A

S

T

A

G

A

A

N

A

V

A

H

S

S

N

V

L

G

D

A

-

I

L

Y
|
Y

Q

F

L

V

T

N

C

S

T

T

F

Y

Y

Y

D

S

A

A

L

L

K

G

Q

C

N

N

D

D

D

Q

A

H

Y

Y

I

I

A

A

R

R

A

A

I

V

Q

Q

L

F

F

F

A

L

P

P

G

G

I

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P

Q

Q

I

V

Y

Y

V

V

G

G

L

A

L

L

A

A

G

G

T

K

N

N

D

D

E

M

E

E

L

L

M

L

E

R

H

K

T

T

G

N

E

N

L

G

R
|
R

D

D

I

I

N

N

R

R

T

H

Y

Y

F

Y

D

S

L

T

E

A

A

E

V

I

A

D

E

E

A

N

T

L

E

K

K

R

P

P

V

V

R

K

R

A

L

L

I

N

Q

A

L

L

L

A

E

K

F

F

R

R

C

N

S

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H

L

P

D

A

A

F

F

R

D

G

G

T

T

F

F

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S

L

Y

V

T

Y

T

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D

N

D

D

D

T

T

S

S

V

I

S

S

M

F

Q

T

W

W

K

R

N

G

G

E

D

T

A

S

K

Q

A

A

L

T

L

L

binding (2~{R},3~{S},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-[3-[(~{E})-2-(4-hydroxyphenyl)ethenyl]-5-oxidanyl-phenoxy]oxane-3,4,5-triol: D50 (= D49), F53 (= F52), P134 (≠ R131), R135 (≠ K132), N192 (≠ D190), A193 (= A191), E232 (= E231), H289 (= H288), D290 (= D289), Y344 (= Y335), R399 (= R390)

6s9uA Crystal structure of sucrose 6f-phosphate phosphorylase from ilumatobacter coccineus (see paper)
31% identity, 97% coverage: 3:467/480 of query aligns to 6:507/520 of 6s9uA

query
sites
6s9uA

L

L

R

P

N

N

L

R

P

V

H

M

L

L

I

N

A

A

Y

Y

P

P

D

D

R

S

M

I

G

D

S

G

S

D

I

L

S

A

D

G

L

T

H

V

K

R

V

M

M

L

-

Q

R

R

E

P

H

E

F

F

P

T

R

D

C

A

F

F

G

G

G

L

V

F

H

Y

L

V

L

L

P

P

P

S

-

I

F

F

P

N

S

S

N

D

A

L

D

D

G

R

G

G

F

F

S

S

P

I

L

I

T

D

H

Y

R

-

E

D

I

L

D

N

P

S

R

D

Y

L

G

A

S

S

W

A

E

E

E

D

V

L

E

A

A

A

L

L

-

D

A

E

A

L

E

G

Y

I

D

M

L

L

C

K

L

F

D

D

L

M

V

V

L

L

N

N

H

H

I

L

A

S

D

V

E

G

S

S

P

P

E

Q

F

F

K

Q

D

D

F

L

L

L

A

K

N

H

G

G

R

D

D

D

S

S

R

A

Y

F

A

R

E

D

L

F

F

F

V

I

D

D

V

W

D

N

A

E

L

F

-

W

-

E

-

G

-

E

G

G

E

E

I

L

T

H

S

A

D

D

D

G

-

H

-

V

-

P

-

S

-

P

-

E

-

H

L

L

A

D

K

R

I

L

H

F

I

M

R
|
R

K

K

E

P

K

G

E

L

P

P

F

I

R

L

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Q

V

V

T

R

L

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A

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N

D

G

G

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K

D

K

R

R

F

V

Y

W

W

C

N

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T

F

F

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V

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I

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-

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Y

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L

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G

Q

Q

V

M

D

D

L

L

N

N

Y

A

D

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A

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P

A

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Y

W

D

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F

F

M

Y

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N

T

L

F

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V

K

M

L

T

A

G

R

H

Y

G

G

V

A

K

K

L

I

F

V

R

R

L

L

D

D

A

A

F

F

G

A

Y

Y

T

L

T

H

K

K

K

A

I

V

G

G

T

D

S

T

C

N

F

F

L

F

V

N

E

T

P

P

D

G

V

T

Y

W

D

D

I

H

L

L

G

D

W

R

F

L

H

R

R

T

T

I

A

S

N

E

R

E

M

N

G

G

A

L

E

V

V

L

L

L

P

P

E
|
E

V

I

H
|
H

D

G

H

E

S

Y

S

G

Y

T

Q

K

F

I

-

H

-

E

A

E

I

L

G

S

M

D

R

R

G

D

M

Y

R

P

P

V

Y

Y

G

D

F

F

A

F

L

F

P

P

P

G

L

L

L

V

L

I

Y

D

S

A

L

I

L

D

D

S

A

A

N

S

S

N

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T

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H

L

L

K

L

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W

W

L

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-

D

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I

C

I

P

E

R

R

N

D

Q

I

I

A

T

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V

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N

-

M

L

L

D

G

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C

H

H

D
|
D

G

G

I

I

C

P

I

V

P

I

D

D

V

L

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K

-

G

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G

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G

G

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L

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Y

A

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A

A

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D

V

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H

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K

V

V

G

-

A

S

I

Y

Y
|
Y

Q

Q

L

V

T

N

C

A

T

T

F

F

Y

F

D

S

A

A

L

L

K

G

Q

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N

S

D

D

D

A

A

R

Y

L

I

R

A

L

A

A

R

R

A

A

I

I

Q

Q

L

L

F

F

A

V

P

P

G

G

I

T

P

P

Q

Q

I

V

Y

W

Y

Y

V

L

G

D

L

L

L

F

A

A

G

G

T

A

N

N

D

D

E

V

E

E

L

A

M

A

E

D

H

R

T

A

G

G

E

A

-

D

-

G

L

H

R

K

D

E

I

I

N

N

R

R

T

T

Y

N

F

L

D

S

L

A

E

A

A

D

V

V

A

E

E

A

A

G

T

L

E

A

K

R

P

P

V

I

V

V

R

L

R

D

L

Q

I

L

Q

E

L

M

L

I

E

R

F

L

R

R

C

N

S

A

H

S

P

P

A

A

F

F

R

D

G

G

T

R

F

F

E

E

L

V

V

V

Y

P

S

T

N

D

D

D

T

T

S

R

V

L

S

Q

M

L

Q

R

W

W

K

Q

N

N

G

G

D

S

A

T

K

V

A

A

L

L

F

D

V

A

D

D

L

L

N

A

F

T

K

E

K

R

T

F

T

T

V

I

R

T

Y

H

binding phosphate ion: R148 (= R131), E260 (= E231), H262 (= H233), D323 (= D289), Y373 (= Y335)

A0A6C7EEG6 Sucrose 6(F)-phosphate phosphorylase; SPP; Sucrose 6'-phosphate phosphorylase; EC 2.4.1.329 from Ilumatobacter coccineus (strain NBRC 103263 / KCTC 29153 / YM16-304) (see paper)
31% identity, 97% coverage: 3:467/480 of query aligns to 10:511/523 of A0A6C7EEG6

query
sites
A0A6C7EEG6

L

L

R

P

N

N

L

R

P

V

H

M

L

L

I

N

A

A

Y

Y

P

P

D

D

R

S

M

I

G

D

S

G

S

D

I

L

S

A

D

G

L

T

H

V

K

R

V

M

M

L

-

Q

R

R

E

P

H

E

F

F

P

T

R

D

C

A

F

F

G

G

G

L

V

F

H

Y

L

V

L

L

P

P

P

S

-

I

F

F

P

N

S

S

N

D

A

L

D

D

G

R

G

G

F

F

S

S

P

I

L

I

T

D

H

Y

R

-

E

D

I

L

D

N

P

S

R

D

Y

L

G

A

S

S

W

A

E

E

E

D

V

L

E

A

A

A

L

L

-

D

A

E

A

L

E

G

Y

I

D

M

L

L

C

K

L

F

D

D

L

M

V

V

L

L

N

N

H

H

I

L

A

S

D

V

E

G

S

S

P

P

E

Q

F

F

K

Q

D

D

F

L

L

L

A

K

N

H

G

G

R

D

D

D

S

S

R

A

Y

F

A

R

E

D

L

F

F

F

V

I

D

D

V

W

D

N

A

E

L

F

-

W

-

E

-

G

-

E

G

G

E

E

I

L

T

H

S

A

D

D

D

G

-

H

-

V

-

P

-

S

-

P

-

E

-

H

L

L

A

D

K

R

I

L

H

F

I

M

R
|
R

K

K

E

P

K

G

E

L

P

P

F

I

R

L

E

Q

V

V

T

R

L

F

A

P

N

D

G

G

E

S

K

D

K

R

R

F

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Y

W

W

C

N

T

T

F

F

T

Y

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K

R

-

V

-

E

-

T

-

I

-

D

-

G

-

E

-

R

-

S

-

Y

-

L

-

G

Q

Q

V

M

D

D

L

L

N

N

Y

A

D

E

A

S

E

P

A

R

T

V

Y

W

D

T

F

F

M

Y

E

R

E

E

N

T

L

F

R

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V

K

M

L

T

A

G

R

H

Y

G

G

V

A

K

K

L

I

F

V

R

R

L

L

D

D

A

A

F

F

G

A

Y

Y

T

L

T

H

K

K

K

A

I

V

G

G

T

D

S

T

C

N

F

F

L

F

V

N

E

T

P

P

D

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V

T

Y

W

D

D

I

H

L

L

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W

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L

H

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T

I

A

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N

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M

N

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G

A

L

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V

L

L

L

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P

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H

D

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Y

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F

I

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H

-

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A

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L

G

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M

D

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R

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D

M

Y

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P

V

Y

Y

G

D

F

F

A

F

L

F

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L

L

L

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L

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D

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A

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L

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H

L

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W

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V

-

N

-

M

L

L

D

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T

C

H

H

D

D

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G

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K

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L

S

L

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-

P

R

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x
K

R

N

R

L

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Y

A

G

A

A

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D

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H

T

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K

V

V

G

-

A

S

I

Y

Y
|
Y

Q

Q

L

V

T

N

C

A

T

T

F

F

Y

F

D

S

A

A

L

L

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G

Q

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D

D

A

A

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Y

L

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A

L

A

A

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R

A

A

I

I

Q

Q

L

L

F

F

A

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P

P

G

G

I

T

P

P

Q

Q

I

V

Y

W

Y

Y

V

L

G

D

L

L

L

F

A

A

G

G

T

A

N

N

D

D

E

V

E

E

L

A

M

A

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D

H

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T

A

G

G

E

A

-

D

-

G

L

H

R
x
K

D

E

I

I

N

N

R

R

T

T

Y

N

F

L

D

S

L

A

E

A

A

D

V

V

A

E

E

A

A

G

T

L

E

A

K

R

P

P

V

I

V

V

R

L

R

D

L

Q

I

L

Q

E

L

M

L

I

E

R

F

L

R

R

C

N

S

A

H

S

P

P

A

A

F

F

R

D

G

G

T

R

F

F

E

E

L

V

V

V

Y

P

S

T

N

D

D

D

T

T

S

R

V

L

S

Q

M

L

Q

R

W

W

K

Q

N

N

G

G

D

S

A

T

K

V

A

A

L

L

F

D

V

A

D

D

L

L

N

A

F

T

K

E

K

R

T

F

T

T

V

I

R

T

Y

H

R152 (= R131) mutation to A: 28-fold decrease in catalytic activity in the synthesis direction, but only slight decrease in affinity for beta-D-fructose 6-phosphate. Gains some activity on fructose, glycerol, and D-glycerate.
K364 (≠ L321) mutation to S: 65-fold decrease in catalytic activity in the synthesis direction, and 3-fold decrease in affinity for beta-D-fructose 6-phosphate. Gains some activity on fructose, glycerol, and D-glycerate.
Y377 (= Y335) mutation to H: 50-fold decrease in catalytic activity in the synthesis direction, but only slight decrease in affinity for beta-D-fructose 6-phosphate.
K434 (≠ R390) mutation to A: 400-fold decrease in catalytic activity in the synthesis direction, and 17-fold decrease in affinity for beta-D-fructose 6-phosphate. Gains some activity on fructose and glycerol.; mutation to R: 6-fold decrease in catalytic activity in the synthesis direction, and 5-fold decrease in affinity for beta-D-fructose 6-phosphate. Gains some activity on fructose and D-glycerate.

D7BAR0 Glucosylglycerate phosphorylase; GGa phosphorylase; GGaP; EC 2.4.1.352 from Allomeiothermus silvanus (strain ATCC 700542 / DSM 9946 / NBRC 106475 / NCIMB 13440 / VI-R2) (Thermus silvanus) (see paper)
29% identity, 87% coverage: 9:427/480 of query aligns to 54:489/555 of D7BAR0

query
sites
D7BAR0

L

L

I

I

A

T

Y

Y

P

G

D

D

R

Q

M

I

G

H

S

A

S

E

-

G

-

E

-

P

I

L

S

Q

D

T

L

L

H

Y

K

D

V

F

M

L

R

Y

E

E

H

R

F

L

P

R

R

G

C

V

F

F

G

S

G

G

V

V

H

H

L

L

P

P

P

F

F

Y

P

P

S

S

N

T

A

S

D

D

G

D

G

G

F

F

S

S

P

V

L

V

T

D

H

F

R

Q

E

R

I

V

D

D

P

P

R

E

Y

L

G

G

S

T

W

W

E

T

E

D

V

I

E

R

A

I

L

I

A

A

A

Q

E

D

Y

F

D

R

L

L

C

M

L

A

D

D

L

L

V

V

L

C

N

N

H

H

I

V

A

S

D

A

E

S

S

S

P

P

E

W

F

F

K

Q

D

G

F

F

L

L

A

Q

N

D

G

-

R

-

D

D

S

P

R

Q

Y

Y

A

Q

E

G

L

F

F

F

V

I

D

T

V

V

D

D

A

P

L

-

G

-

E

-

I

-

T

-

S

G

D

T

D

D

L

L

A

S

K

T

I

V

H

-

I

F

R

R

K

P

E

R

K

A

E

L

P

P

F

L

R

L

E

T

V

P

T

F

L

Q

A

T

N

P

G

S

E

G

K

E

K

K

R

L

V

V

W

W

C

T

T

T

F

F

T

S

E

P

K

D

Q

Q

V

T

D

D

L

L

N

N

Y

Y

D

A

A

N

E

P

A

E

T

V

Y

L

D

L

F

E

M

V

E

I

E

E

N

A

L

L

R

L

V

C

M

Y

T

V

G

R

H

N

G

G

V

A

K

G

L

L

F

I

R

R

L

L

D

D

A

A

F

V

G

G

Y

F

T

I

T

W

K

K

K

E

I

I

G

G

T

T

S

S

C

C

F

M

L

H

V

L

E

E

P

-

D

G

V

A

Y

H

D

R

I

I

L

V

G

K

W

L

F

M

H

R

R

L

T

V

A

L

N

D

R

A

M

V

G

A

A

P

E

H

V

V

L

L

P

L

E

V

V

S

H

E

D

T

H
x
N

S

A

S

P

Y

H

Q

R

F

E

A

N

I

I

G

S

M

Y

R

F

G

G

-

N

-

G

-

H

-

D

-

E

-

A

M

Q

R

L

P

V

Y

Y

G

Q

F

F

A

P

L

L

P

P

L

L

L

V

L

M

Y

H

S

T

L

F

L

R

D

T

A

G

N

D

S

A

V

S

H

K

L

L

K

A

N

G

W

W

L

A

R

A

-

G

-

L

V

T

C

L

P

P

R

S

N

E

Q

R

I

T

T

T

-

F

-

N

V

F

L

L

D

A

T

S

H

H

D

D

G

G

I

I

C

G

I

V

P

V

D

P

V

A

E

G

G

G

I

I

L

L

P

Q

A

P

D

E

K

E

I

I

Q

A

A

A

V

L

I

V

D

R

N

Q

V

A

S

L

Q

E

R

H

S

G

A

G

D

-

P

-

I

-

L

-

R

R

R

V

S

N

A

H

A

K

N

D

V

T

H

P

S

D

V

G

G

P

A

V

I

P

Y

Y

Q
x
E

L

L

T

C

C

L

T

T

F

L

Y

F

D

D

A

A

L

L

K

S

-

N

-

P

Q

N

N

S

D

D

D

E

A

A

-

E

-

D

-

L

-

K

-

I

-

A

-

R

Y

F

I

L

A

A

R

N

A

V

I

I

Q

L

L

L

F

S

A

L

P

Q

G

G

I

I

P

P

Q

G

I

V

Y

Y

Y

I

V

H

G

S

L

L

L

F

A

G

G

S

T

P

N

S

D

D

E

H

E

A

L

G

M

F

E

E

H

E

T

S

G

G

E

I

L

P

R

R

D

R

I

L

N

N

R

R

T

H

Y

K

F

F

D

T

L

K

E

A

A

E

V

L

A

E

E

E

A

R

T

L

E

A

K

D

P

P

V

A

V

S

R

R

-

A

-

K

-

I

-

L

-

A

R

A

L

Y

I

S

Q

H

L

L

E

R

F

V

R

R

C

S

S

M

H

H

P

P

A

A

F

F

N275 (≠ H235) mutation to A: 75-fold decrease in catalytic activity.; mutation to H: 38-fold decrease in catalytic activity.
E383 (≠ Q336) mutation E->A,Q: More than 100-fold decrease in catalytic activity.

3czkA Crystal structure analysis of sucrose hydrolase(suh) e322q-sucrose complex (see paper)
29% identity, 41% coverage: 7:204/480 of query aligns to 84:289/618 of 3czkA

query
sites
3czkA

P

P

H

H

L

M

I

L

-

G

-

Y

-

S

A

A

Y

Y

P

A

D

D

R

R

M

F

G

A

S

G

S

T

I

L

S

Q

D

G

L

V

H

A

K

E

V

-

M

-

R

R

E

V

H

P

F

Y

P

L

R

Q

C

E

F

L

G

G

G

V

-

R

-

Y

V

L

H

H

L

L

P

P

P

F

F

L

P

R

S

A

N

R

A

A

-

G

-

D

-

N

D
|
D

G

G

F
|
F

S

A

P

V

L

S

T

D

H

Y

R

G

E

Q

I

V

D

E

P

P

R

S

Y

L

G

G

S

S

W

N

E

D

V

L

E

V

A

A

L

L

A

T

-

S

-

R

-

L

-

R

-

E

A

A

E

G

Y

I

D

S

L

L

C

C

L

A

D
|
D

L

F

V

V

L

L

N

N

H
|
H

I

T

A

A

D

D

E

D

S

H

P

A

E

W

F

A

K

Q

D

-

F

-

L

A

A

A

N

R

G

A

R

G

D

D

S

A

R

R

Y

Y

A

L

E

D

L

Y

F

Y

V

-

D

-

V

-

D

H

A

H

L

F

G

A

E

D

I

R

T

T

S

V

D

P

D

D

-

R

-

Y

-

E

-

A

-

T

L

L

A

G

K

Q

I

V

H

F

I

P

R

H

K

T

E

A

K

P

E

G

P

N

F

F

R

-

E

-

V

-

T

T

L

W

A

V

N

D

G

D

E

T

K

A

K

Q

R

W

V

M

W

W

C

T

T

T

F
|
F

T

Y

E

P

K

Y

Q

Q

V

W

D

D

L

L

N

N

Y

W

D

S

A

N

E

P

A

A

T

V

Y

F

D

G

F

D

M

M

E

A

E

L

N

A

L

M

R

L

V

R

M

L

T

A

G

N

H

L

G

G

V

V

K

E

L

A

F

F

R
|
R

L

L

D
|
D

A

S

F

T

G

A

Y

Y

T

L

T

W

K

K

K

R

I

I

G

G

T

T

S

D

C

C

F

M

active site: D170 (= D82), D275 (= D190)
binding beta-D-fructofuranose: F239 (= F154)
binding alpha-D-glucopyranose: D132 (= D49), F135 (= F52), H175 (= H87), F239 (= F154), R273 (= R188), D275 (= D190)

Sites not aligning to the query:

active site: 317, 386, 387
binding beta-D-fructofuranose: 317, 387, 388
binding alpha-D-glucopyranose: 317, 386, 387, 506

3uerA Crystal structure of amylosucrase from deinococcus geothermalis in complex with turanose (see paper)
28% identity, 43% coverage: 10:213/480 of query aligns to 100:311/651 of 3uerA

query
sites
3uerA

I

V

A

A

Y

Y

P

T

D

D

R

R

M

F

G

A

S

G

S

T

I

L

S

K

D

G

L

V

H

E

K

E

V

R

M

L

R

D

E

Y

H

L

F

E

P

G

R

L

C

G

F

V

G

K

G

Y

V

L

H

H

L

L

L

M

P

P

-

L

-

R

P

P

F

R

P

E

S

G

N

E

A

N

D
|
D

G

G

F
x
Y

S

A

P

V

L

Q

T

D

H

Y

R

R

E

A

I

V

D

R

P

P

R

D

Y

L

G

G

S

T

W

M

E

D

V

L

E

S

A

A

L

L

A

A

A

R

E

A

Y

L

-

R

-

G

-

R

-

G

-

I

D

S

L

L

C

V

L

L

D
|
D

L

L

V

V

L

L

N

N

H
|
H

I

V

A

A

D

R

E

E

S

H

P

A

E

W

F

A

K

Q

D

K

F

A

L

R

A

A

N

G

G

D

R

P

D

K

S

Y

R

R

-

A

Y

Y

A

F

E

H

L

L

F

F

V

P

D

D

V

R

D

R

A

G

L

P

G

D

E

A

I

F

T

E

S

A

D

T

D

-

L

L

A

P

K

E

I

I

H

F

I

P

R

D

K

F

E

A

K

P

E

G

P

N

F

F

R

S

-

W

E

D

V

E

T

E

L

I

A

G

N

E

G

G

E

E

K

G

R

W

V

V

W

W

C

T

T

T

F
|
F

T

N

E

S

K

Y

Q

Q

V

W

D

D

L

L

N

N

Y

W

D

A

A

N

E

P

A

D

T

V

Y

F

D

L

F

E

M

F

E

V

E

D

N

I

L

I

R

L

V

Y

M

L

T

A

G

N

H

R

G

G

V

V

K

E

L

V

F

F

R

R

L

L

D
|
D

A
|
A

F

I

G

A

Y
x
F

T

I

T

W

K

K

K

R

I

L

G

G

T

T

S

D

C

C

F

-

L

Q

V

N

E

Q

P

P

D

E

V

V

Y

H

D

H

I

L

active site: D180 (= D82), D289 (= D190)
binding beta-D-fructofuranose: F253 (= F154), F293 (≠ Y194)
binding alpha-D-glucopyranose: D142 (= D49), D142 (= D49), Y145 (≠ F52), Y145 (≠ F52), H185 (= H87), H185 (= H87), F253 (= F154), F253 (= F154), D289 (= D190), D289 (= D190)
binding alpha-D-fructofuranose: F253 (= F154), A290 (= A191), F293 (≠ Y194)

Sites not aligning to the query:

active site: 331, 400, 401
binding beta-D-fructofuranose: 331, 333, 401
binding alpha-D-glucopyranose: 400, 400, 401, 401, 525, 525
binding alpha-D-fructofuranose: 331, 401

4lxfB Crystal structure of m. Tuberculosis tres (see paper)
28% identity, 34% coverage: 41:203/480 of query aligns to 77:240/546 of 4lxfB

query
sites
4lxfB

L

L

P

P

F

F

P

Y

S

D

N

S

A

P

-

L

-

R

D

D

G

G

F

Y

S

D

P

I

L

R

T

D

H

F

R

Y

E

K

I

V

D

L

P

P

R

E

Y

F

G

G

S

T

W

V

E

D

V

F

E

V

A

A

L

L

A

V

A

D

E

A

-

A

-

H

-

R

-

G

Y

I

D

R

L

I

C

I

L

T

D

D

L

L

V

V

L

M

N
|
N

H

H

I

T

A

S

D

E

E

S

S

H

P

P

E

W

F

F

K

Q

D

E

F

S

L

R

A

R

N

D

G

-

R

P

D

D

S

G

R

P

Y

Y

A

G

E

D

L

Y

F

Y

V

V

D

W

V

S

D

D

A

T

L

S

G

E

E

R

I

Y

T

T

S

D

D

A

D

R

L

I

A

I

K

F

I

V

H

D

I

T

R

E

K

E

E

S

K

N

E

W

P

S

F

F

R

D

E

P

V

V

T

-

L

-

A

-

N

-

G

-

E

R

K

R

K

Q

R

F

V

Y

W

W

C

H

T

R

F

F

T

F

E

S

K

H

Q

Q

V

P

D
|
D

L

L

N

N

Y

Y

D

D

A

N

E

P

A

A

T

V

Y

Q

D

E

F

A

M

M

E

I

E

D

N

V

L

I

R

R

V

F

M

W

T

L

G

G

H

L

G

G

V

I

K

D

L

G

F

F

R

R

L

L

D

D

A

A

F

V

G

P

Y
|
Y

T
x
L

T

F

K
x
E

K

R

I

E

G

G

T

T

S

N

C

C

binding calcium ion: N129 (= N86), D197 (= D160), Y231 (= Y194), L232 (≠ T195), E234 (≠ K197)

8uzhB Sumo fused trehalose synthase (tres) of mycobacterium tuberculosis (see paper)
28% identity, 34% coverage: 41:203/480 of query aligns to 128:291/626 of 8uzhB

query
sites
8uzhB

L

L

P

P

F

F

P

Y

S

D

N

S

A

P

-

L

-

R

D

D

G

G

F

Y

S

D

P

I

L

R

T

D

H

F

R

Y

E

K

I

V

D

L

P

P

R

E

Y

F

G

G

S

T

W

V

E

D

V

F

E

V

A

A

L

L

A

V

A

D

E

A

-

A

-

H

-

R

-

G

Y

I

D

R

L

I

C

I

L

T

D

D

L

L

V

V

L

M

N
|
N

H

H

I

T

A

S

D

E

E

S

S

H

P

P

E

W

F

F

K

Q

D

E

F

S

L

R

A

R

N

D

G

P

R

-

D

D

S

G

R

P

Y

Y

A

G

E

D

L

Y

F

Y

V

V

D

W

V

S

D

D

A

T

L

S

G

E

E

R

I

Y

T

T

S

D

D

A

D

R

L

I

A

I

K

F

I

V

H

D

I

T

R

E

K

E

E

S

K

N

E

W

P

S

F

F

R

D

E

P

V

V

T

-

L

-

A

-

N

-

G

-

E

R

K

R

K

Q

R

F

V

Y

W

W

C

H

T

R

F

F

T

F

E

S

K

H

Q

Q

V

P

D
|
D

L

L

N

N

Y

Y

D

D

A

N

E

P

A

A

T

V

Y

Q

D

E

F

A

M

M

E

I

E

D

N

V

L

I

R

R

V

F

M

W

T

L

G

G

H

L

G

G

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I

K

D

L

G

F

F

R

R

L

L

D

D

A

A

F

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G

P

Y
|
Y

T
x
L

T

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x
E

K

R

I

E

G

G

T

T

S

N

C

C

binding calcium ion: N180 (= N86), D248 (= D160), Y282 (= Y194), L283 (≠ T195), E285 (≠ K197)

Q9ZEU2 Amylosucrase; EC 2.4.1.4 from Neisseria polysaccharea (see 2 papers)
26% identity, 35% coverage: 38:203/480 of query aligns to 138:307/636 of Q9ZEU2

query
sites
Q9ZEU2

V

L

H

H

L

L

L

M

P

P

P

L

F

F

P

K

-

C

-

P

-

E

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N

K

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D

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G

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Y

S

A

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Y

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N

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P

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-

R

E

E

A

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A

A

E

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E

L

A

-

G

-

I

-

S

-

A

C

V

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D

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F

N

N

H
|
H

I

T

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N

E

E

-

H

-

E

-

W

-

A

-

Q

-

R

-

C

-

A

-

G

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P

E

L

F

F

K

D

D

N

F

F

L

Y

A

Y

N

I

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D

D

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R

R

R

Y

M

A

P

E

D

L

Q

F

Y

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-

D

-

V

-

D

-

A

-

L

-

G

-

E

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I

-

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-

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A

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E

I

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E

H

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P

F

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G

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F

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T

Q

L

L

A

E

N

D

G

G

E

-

K

-

K

R

R

W

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V

W

W

C

T

T

T

F

F

T

N

E

S

K

F

Q

Q

V

W

D

D

L

L

N

N

Y

Y

D

S

A

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E

P

A

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Y

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D

R

F

A

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M

E

A

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N

E

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M

R

L

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F

M

L

T

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N

H

L

G

G

V

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D

L

I

F

L

R

R

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D
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D

A

A

F

V

G

A

Y

F

T

I

T

W

K

K

K

Q

I

M

G

G

T

T

S

S

C

C

H195 (= H87) mutation to Q: 98% reduction of activity.
D294 (= D190) active site, Nucleophile; mutation D->E,N: Complete loss of activity.

Sites not aligning to the query:

308 E→Q: No effect.
336 E→Q: Complete loss of activity.
352 E→Q: 30% reduction of activity.
400 H→N: 97% reduction of activity.
401 D→E: Almost complete loss of activity.

3ueqA Crystal structure of amylosucrase from neisseria polysaccharea in complex with turanose (see paper)
26% identity, 35% coverage: 38:203/480 of query aligns to 134:303/632 of 3ueqA

query
sites
3ueqA

V

L

H

H

L

L

L

M

P

P

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L

F

F

P

K

-

C

-

P

-

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N

K

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D

G

G

F
x
Y

S

A

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S

H

Y

R

R

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I

V

D

N

P

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-

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E

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A

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I

A

A

E

L

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E

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A

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G

-

I

-

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-

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C

V

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D

L

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F

N

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H

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D

N

E

E

-

H

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-

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C

-

A

-

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L

F

F

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D

D

N

F

F

L

Y

A

Y

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I

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D

D

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M

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-

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-

V

-

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I

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L

A

E

N

D

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G

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-

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R

W

V

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W

C

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F
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F

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N

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F

Q

Q

V

W

D

D

L

L

N

N

Y

Y

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A

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V

Y

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D

R

F

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M

M

E

A

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N

E

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T

A

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L

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G

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D

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R

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D
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D

A
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A

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M

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G

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T

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S

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C

active site: D186 (= D82), R288 (= R188), D290 (= D190)
binding 3-O-alpha-D-glucopyranosyl-D-fructose: D148 (= D49), Y151 (≠ F52), H191 (= H87), I232 (= I130), F254 (= F154), D290 (= D190), A291 (= A191)

Sites not aligning to the query:

active site: 332, 396, 397
binding alpha-D-glucopyranose: 563, 564
binding 3-O-alpha-D-glucopyranosyl-D-fructose: 332, 334, 396, 397, 513

8uqvA Trehalose synthase (tres) of mycobacterium tuberculosis in complex with 6-treaz compound (see paper)
27% identity, 34% coverage: 41:203/480 of query aligns to 49:212/547 of 8uqvA

query
sites
8uqvA

L

L

P

P

F

F

P

Y

S

D

N

S

A

P

-

L

-

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D
|
D

G

G

F
x
Y

S

D

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I

L

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F

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A

L

L

A

V

A

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E

A

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A

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I

C

I

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D

L

L

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N

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S

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E

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N

D

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P

R

-

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D

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G

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Y

Y

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D

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Y

F

Y

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V

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D

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A

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I

Y

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T

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D

D

A

D

R

L

I

A

I

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F

I

V

H

D

I

T

R

E

K

E

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S

K

N

E

W

P

S

F

F

R

D

E

P

V

V

T

-

L

-

A

-

N

-

G

-

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K

Q

R

F

V

Y

W
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W

C

H

T

R

F

F

T

F

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S

K

H

Q

Q

V

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D
|
D

L

L

N

N

Y

Y

D

D

A

N

E

P

A

A

T

V

Y

Q

D

E

F

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M

M

E

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D

N

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R

V

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M

W

T

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G

G

H

L

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G

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R

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L

D

A

A

A

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|
Y

T
x
L

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x
E

K

R

I

E

G

G

T

T

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N

C

C

binding calcium ion: W160 (= W151), D169 (= D160), Y203 (= Y194), L204 (≠ T195), E206 (≠ K197)
binding alpha-D-glucopyranose: D59 (= D49), Y62 (≠ F52)

Sites not aligning to the query:

9ezlA Crystal structure of trehalose synthase mutant n253h from deinococcus radiodurans (see paper)
29% identity, 40% coverage: 40:233/480 of query aligns to 48:248/548 of 9ezlA

query
sites
9ezlA

L

L

P

P

P

W

F

F

P

P

S

S

N

P

A

L

-

R

D

D

G

D

G

G

F

Y

S

D

P

V

L

A

T

D

H

Y

R

R

E

G

I

I

D

H

P

P

R

D

Y

L

G

G

S

T

W

L

E

D

V

F

-

K

-

V

-

F

-

L

-

R

E

E

A

A

L

H

A

A

A

R

E

G

Y

L

D

W

L

V

C

I

L

G

D

D

L

L

V

V

L

T

N
|
N

H

H

I

T

A

S

D

S

E

D

S

H

P

P

E

W

F

F

K

Q

-

A

-

R

-

G

D

P

F

T

L

L

A

P

N

D

G

G

R

S

D

P

S

N

R

E

Y

Y

A

H

E

D

L

Y

F

Y

V

V

D

W

V

S

D

D

A

E

L

-

G

-

E

-

I

-

T

-

S

G

D

K

D

E

L

Y

A

A

K

D

I

T

H

R

I

I

R

I

K

F

E

T

K

D

E

T

P

E

F

V

R

S

E

N

V

W

T

T

L

L

A

D

N

E

G

Q

E

A

K

G

K

K

R

Y

V

Y

W

W

C

H

T

R

F

F

T

F

E

A

K

S

Q

Q

V

P

D
|
D

L

L

N

N

Y

Y

D

D

A

N

E

P

A

K

T

V

Y

V

D

E

F

E

M

L

E

H

E

G

N

A

L

A

R

R

V

F

M

W

T

L

G

D

H

L

G

G

V

L

K

D

L

G

F

F

R

R

L

V

D

D

A

A

F

V

G

P

Y
|
Y

T
x
L

T

I

K
x
E

K

R

I

E

G

G

T

T

S

S

C

C

F

E

L

N

V

L

E

-

P

P

D

E

V

T

Y

H

D

E

I

I

L

L

G

K

W

G

F

F

H

R

R

A

T

M

A

V

N

D

R

R

M

E

-

Y

-

P

G

G

A

R

E

L

V

L

L

L

P

A

E

E

V

A

H

H

binding calcium ion: N100 (= N86), D174 (= D160), Y208 (= Y194), L209 (≠ T195), E211 (≠ K197)

Sites not aligning to the query:

binding magnesium ion: 21, 23, 25, 27

Query Sequence

>WP_043766493.1 NCBI__GCF_000733765.1:WP_043766493.1
MILRNLPHLIAYPDRMGSSISDLHKVMREHFPRCFGGVHLLPPFPSNADGGFSPLTHREI
DPRYGSWEEVEALAAEYDLCLDLVLNHIADESPEFKDFLANGRDSRYAELFVDVDALGEI
TSDDLAKIHIRKEKEPFREVTLANGEKKRVWCTFTEKQVDLNYDAEATYDFMEENLRVMT
GHGVKLFRLDAFGYTTKKIGTSCFLVEPDVYDILGWFHRTANRMGAEVLPEVHDHSSYQF
AIGMRGMRPYGFALPPLLLYSLLDANSVHLKNWLRVCPRNQITVLDTHDGICIPDVEGIL
PADKIQAVIDNVSQRSADPILRRSAANVHSVGAIYQLTCTFYDALKQNDDAYIAARAIQL
FAPGIPQIYYVGLLAGTNDEELMEHTGELRDINRTYFDLEAVAEATEKPVVRRLIQLLEF
RCSHPAFRGTFELVYSNDTSVSMQWKNGDAKALLFVDLNFKKTTVRYRDERTGRMISRIF

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory