SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_053768266.1 NCBI__GCF_001280255.1:WP_053768266.1 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 6 hits to proteins with known functional sites (download)

A0RV30 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; EC 3.1.3.11; EC 4.1.2.13 from Cenarchaeum symbiosum (strain A) (see 2 papers)
54% identity, 100% coverage: 1:362/363 of query aligns to 1:357/376 of A0RV30

query
sites
A0RV30

M

M

R

R

I

I

T

T

L

V

S

S

V

A

L

I

K

K

A

A

D

D

I

V

G

G

S

G

V

I

G

G

H

H

T

T

L

L

P

P

S

S

P

S

A

G

V

L

L

L

A

D

A

A

V

V

K

R

E

R

V

K

V

V

E

S

A

S

K

-

G

-

S

S

L

L

L

I

D

D

A

H

Y

Y

V

I

F

G

H

Y

I

C

G

G

D

D

I

V

V

H

L

I

L

V

L

M

S

T

H

H

T

T

Q

R

G

G

V

T

A

D

H

N

P

S

A

D

I

I

H

H

E

K

L

L

A

A

W

W

K

D

A

A

F

F

R

M

E

E

G

G

T

T

E

R

V

V

A

A

K

K

R

E

E

E

G

G

L

L

Y

Y

G

G

A

A

G

G

Q

Q

D

D

L

L

K

R

D

D

A

S

F

F

T

S

G

G

N

N

L

V

H

K

G

G

L

M

G

G

P

P

Q

G

V

V

A

A

E

E

M

L

E

E

F

F

A

E

E

E

R

R

P

A

S

N

E

E

P

A

F

F

M

T

V

V

L

F

A

A

D

D

K

K

T

T

E

E

P

P

G

G

A

A

F

F

N

N

L

Y

P

P

L

F

Y

Y

L

R

A

M

F

F

A

V

D

D

P

S

M

L

Y

S

S

N

S

T

G

G

L

L

L

I

L

V

S

N

P

K

E

S

L

L

R

A

P

E

G

G

F

V

R

V

F

I

R

N

I

I

M

M

D

D

L

V

-

S

-

K

A

A

Q

R

T

T

E

A

R

R

D

L

S

V

Y

L

I

W

E

E

L

-

D

D

A

K

P

P

E

T

R

-

L

-

Y

-

D

-

I

I

A

E

A

A

L

A

L

L

R

M

D

Y

S

P

H

G

R

R

F

F

A

V

I

V

A

S

S

S

I

V

W

E

L

T

R

R

K

D

Y

-

G

G

E

E

V

P

A

I

A

A

V

S

V

A

S

S

T

T

T

D

R

R

L

L

R

H

N

N

I

I

A

A

G

G

R

T

Y
|
Y

V

V

G

G

K
|
K

D
|
D

D

D

P

P

V

I

A

C

L

L

V

V

R

R

T

T

Q

Q

K

K

I

R

F

F

P

P

A

A

T

T

E

E

F

A

G

G

P

S

P

C

F

F

A

N

L

N

A

P

P

H

F

Y

V

V

A

A

G

G

D

N

T

T

R

R

G

G

S

S

H

H

L

M

P

P

L

L

M

M

P

P

V

V

K

R

A

L

N

N

T

S

P

P

A

A

S

S

T

I

F

N

F

F

C

C

V

I

P

P

M

I

V

V

C

E

A

A

L

L

G

V

F

F

S

S

L

M

K

H

E

E

G

G

R

R

L

L

T

T

G

G

P

P

V

F

D

D

L

G

F

F

A

S

D

T

P

P

V

D

W

W

D

D

A

D

V

V

R

R

A

R

K

T

V

A

V

T

E

R

K

R

A

A

Q

H

E

A

M

M

R

R

Q

Q

G

G

F

F

Y

V

G

H

P

P

A

A

M

T

L

L

P

V

M

P

E

D

E

E

L

L

E
|
E

Y
|
Y

T

A

-

E

G

G

I

Y

A

R

E

S

R

R

L

M

K

D

E

V

L

L

E

D

R

S

E

K

F

M

Y224 (= Y230) mutation to F: Shows slightly decreased FBP phosphatase activity, whereas FBP aldolase activity is nearly completely abolished.
K227 (= K233) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity; mutation to R: Shows enhanced FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
D228 (= D234) mutation to N: Shows completely abolition of both FBP aldolase and FBP phosphatase activities.
E341 (= E347) mutation to Q: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished.
Y342 (= Y348) mutation to F: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished.

F9VMT6 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; Fructose-1,6-bisphosphatase; FBPase; EC 3.1.3.11; EC 4.1.2.13 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 2 papers)
47% identity, 100% coverage: 1:363/363 of query aligns to 1:362/384 of F9VMT6

query
sites
F9VMT6

M

M

R

K

I

T

T

T

L

I

S

S

V

V

L

I

K

K

A

A

D
|
D

I

I

G

G

S

S

V

L

G

A

G

G

H
|
H

T

H

L

I

P

V

S

H

P

P

A

D

V

T

L

M

A

A

V

A

K

N

E

K

V

V

V

L

E

A

E

S

A

A

K

K

-

E

G

Q

S

G

L

I

L

L

D

D

A

Y

Y

Y

V

I

F

T

H

H

I

V

G

G

D
|
D

I

L

V

Q

L

L

L

I

L

M

S

T

H

H

T

T

Q

R

G

G

V

E

A

L

H

D

P

T

A

K

I

V

H

H

E

E

L

T

A

A

W

W

K

N

A

A

F

F

R

K

E

E

G

A

T

A

E

K

V

V

A

A

K

K

R

D

E

L

G

G

L

L

Y
|
Y

G

A

A

A

G

G

Q
|
Q

D

D

L

L

K

S

D

D

A

S

F

F

T

S

G
|
G

N
|
N

L

V

H

R

G

G

L

L

G

G

P

P

Q

G

V

V

A

A

E

E

M

M

E

E

F

I

A

E

E

E

R

R

P

A

S

S

E

E

P

P

F

I

M

A

V

I

L

F

A

M

A

A

D
|
D

K
|
K

T

T

E

E

P

P

G

G

A

A

F

Y

N

N

L

L

P

P

L

L

Y

Y

L

K

A

M

F

F

A

A

D

D

P

P

M

F

Y

N

S

T

S

P

G

G

L

L

L

V

L

I

S

D

P

P

E

T

L

M

R

H

P

G

G

G

F

F

R

K

F

F

R

E

I

V

M

L

D

D

L

V

A

Y

Q

Q

T

G

E

E

R

A

D

-

S

-

Y

-

I

V

E

M

L

L

D

S

A

A

P

P

E

Q

R

E

L

I

Y

Y

D

D

I

L

A

L

A

A

L

L

L

I

R

G

D

T

S

P

H

A

R

R

F

Y

A

V

I

I

A

R

S

R

I

V

W

Y

L

R

R

N

K

E

Y

D

G

N

E

L

V

L

A

A

V

V

S

S

T

I

T

E

R

R

L

L

R

N

N

L

I

I

A

A

G

G

R

K

Y
|
Y

V

V

G

G

K
|
K

D
|
D

P

P

V

V

A

M

L

I

V

V

R

R

T

L

Q
|
Q

K
x
H

I

G

F

L

P

P

A

A

T

L

E

G

E

E

F

A

G

L

P

E

P

A

F

F

A

A

L

F

A

P

P

H

F

L

V

V

A

P

G

G

D

W

T

M

R
|
R

G

G

S

S

H

H

H

Y

L

G

P

P

L

L

M

M

P

P

V

V

-

S

K

Q

A

R

N

D

T

A

P

K

A

A

S

T

T

R

F

F

F
x
D

C

G

V

P

P

P

M

R

V

L

C

L

A

G

L

L

G

G

F

F

S

N

L

V

K

K

E

N

G

G

R

R

L

L

T

V

G

G

P

P

V

T

D

D

L

L

F

F

A

D

D

D

P

P

V

A

W

F

D

D

A

E

V

T

R

R

A

R

K

L

V

A

V

N

E

I

K

V

A

A

Q

D

E

Y

M

M

R

R

Q

H

G

G

F

P

Y

F

G

M

P

P

A

H

M

R

L

L

P

E

M

P

E

T

E

E

L

M

E

E

Y
|
Y

T

T

G

T

I

L

A

P

E

L

R

I

L

L

K

E

E

K

L

L

E

K

R

D

E

R

F

F

S

K

D11 (= D11) binding Mg(2+); mutation to A: 930-fold decrease in FBPase catalytic efficiency.
H18 (= H18) binding in other chain; binding dihydroxyacetone phosphate; binding Mg(2+); mutation to A: 1.7-fold increase in FBPase catalytic activity and 5-fold decrease in FBP affinity, leading to a 2.7-fold decrease in FBPase catalytic efficiency.
D52 (= D51) binding Mg(2+); binding Mg(2+); mutation to A: 175-fold decrease in FBPase catalytic efficiency.
D53 (= D52) binding Mg(2+); mutation to A: 1000-fold decrease in FBPase catalytic activity.
Y90 (= Y89) binding in other chain
Q94 (= Q93) binding Mg(2+); mutation to A: 1.3-fold increase in FBPase catalytic efficiency.
GN 103:104 (= GN 102:103) binding in other chain
D131 (= D130) binding Mg(2+); mutation to A: 2-fold increase in FBP affinity and 10-fold decrease in FBPase catalytic activity, leading to a 5.5-fold decrease in FBPase catalytic efficiency.
K132 (= K131) binding in other chain; binding dihydroxyacetone phosphate
Y228 (= Y230) mutation to F: Retains the FBPase activity, but loses the FBP aldolase activity.
K231 (= K233) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity; binding Mg(2+)
D232 (= D234) binding Mg(2+); binding Mg(2+); mutation to A: 275-fold decrease in FBPase catalytic activity.
D233 (= D235) binding Mg(2+); binding Mg(2+); mutation to A: 2000-fold decrease in FBPase catalytic activity.
QH 241:242 (≠ QK 243:244) binding beta-D-fructose 1,6-bisphosphate
R265 (= R267) binding in other chain; binding dihydroxyacetone phosphate
D286 (≠ F287) binding in other chain; binding dihydroxyacetone phosphate
Y347 (= Y348) binding in other chain

3t2dA Fructose-1,6-bisphosphate aldolase/phosphatase from thermoproteus neutrophilus, fbp-bound form (see paper)
48% identity, 99% coverage: 1:359/363 of query aligns to 1:369/390 of 3t2dA

query
sites
3t2dA

M

M

R

R

I

V

T

T

L

V

S

S

V

I

L

I

K

K

A

A

D
|
D

I

V

G

G

S

G

V

F

G

P

G

G

H
|
H

T

A

L

H

P

V

S

H

P

P

A

K

V

M

L

L

A

E

-

Y

A

A

V

A

K

A

E

K

V

L

V

K

E

E

E

A

A

Q

K

K

G

R

S

G

L

V

L

I

D

D

A

Y

Y

F

V

V

F

Y

H

N

I

V

G

G

D
|
D

I

I

V

S

L

L

L

M

S

T

H

H

T

T

Q

K

G

G

V

E

A

D

H

N

P

K

A

D

I

I

H

H

E

G

L

L

A

A

W

W

K

E

A

T

F

F

R

K

E

E

G

V

T

T

-

D

E

Q

V

I

A

A

K

K

R

R

E

F

G

K

L

L

Y
|
Y

G

G

A

A

G

G

Q
|
Q

D

D

L

L

K

K

D

D

A

A

F

F

T
x
S

G
|
G

N
|
N

L

I

H

R

G

G

L

M

G

G

P

P

Q

Q

V

V

A

A

E

E

M

M

E

E

F

F

A

E

E

E

R

R

P

P

S

S

E

E

P

P

F

I

M

I

V

A

L

F

A

A

D
|
D

K
|
K

T

T

E

E

P

P

G

G

A

A

F

F

N

N

L

L

P

P

L

L

Y

Y

L

K

A

M

F

F

A

A

D

D

P

P

M

F

Y

T

S

T

S

A

G

G

L

L

L

V

L

I

S

D

P

P

E

S

L

M

R

H

P

E

G

G

F

F

R

I

F

F

R

E

I

V

M

L

D

D

L

V

A

-

Q

-

T

V

E

E

R

H

D

K

S

V

Y

Y

I

L

E

-

L

L

D

K

A

T

P

P

E

E

R

D

L

A

Y

Y

D

S

I

L

A

L

A

G

L

L

L

I

R

G

D

T

S

T

H

G

R

R

F

Y

A

I

I

I

A

R

S

K

I

V

W

F

L

R

R

R

K

A

Y

D

G

G

E

A

V

P

A

A

V

A

V

N

S

S

T

V

T

E

R

R

L

L

R

S

N

L

I

I

A

A

G

G

R

R

Y

Y

V

V

G

G

K

K

D
|
D

P

P

V

V

A

L

L

L

V

V

R

R

T

A

Q

Q

K

S

I

G

F

L

P

P

A

A

T

V

E

G

E

E

F

V

G

L

P

E

P

A

F

F

A

A

L

H

A

P

P

H

F

L

V

V

A

H

G

G

D

W

T
x
M

R
|
R

G

G

S

S

H

H

H

A

L

G

P

P

L

L

M

M

P

P

V

A

K

R

-

F

-

I

-

S

-

V

-

D

-

P

-

E

-

R

-

I

A

A

N

I

T

G

P

P

A

K

S

M

T

T

F

R

F

F

-
x
D

C

G

V

P

P

P

M

K

V

V

C

G

A

A

L

L

G

G

F

F

S

Q

L

L

K

H

E

E

G

G

R

Y

L

L

T

E

G

G

P

G

V

V

D

D

L

L

F

F

A

D

D

D

P

P

V

A

W

F

D

D

A

Y

V

V

R

R

A

Q

K

T

V

A

E

Q

K

I

A

A

Q

D

E

Y

M

I

R

R

Q

M

G

G

F

P

Y

F

G

Q

P

P

A

H

M

R

L

L

P

P

M

P

E

E

L

M

E

E

Y
|
Y

T

T

G

A

I

L

A

P

E

K

R

I

L

L

K

A

E

K

L

V

E

K

binding magnesium ion: D11 (= D11), H18 (= H18), D52 (= D51), D52 (= D51), D53 (= D52), Q95 (= Q93), D132 (= D130), D233 (= D234), D234 (= D235), D234 (= D235)
binding 1,6-di-O-phosphono-D-fructose: H18 (= H18), D52 (= D51), Y91 (= Y89), Q95 (= Q93), S103 (≠ T101), G104 (= G102), N105 (= N103), K133 (= K131), D233 (= D234), D234 (= D235), M265 (≠ T266), R266 (= R267), D297 (vs. gap), Y358 (= Y348)

B1YAL1 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; EC 3.1.3.11; EC 4.1.2.13 from Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta) (Thermoproteus neutrophilus) (see paper)
48% identity, 99% coverage: 1:359/363 of query aligns to 1:369/399 of B1YAL1

query
sites
B1YAL1

M

M

R

R

I

V

T

T

L

V

S

S

V

I

L

I

K

K

A

A

D
|
D

I

V

G

G

S

G

V

F

G

P

G

G

H
|
H

T

A

L

H

P

V

S

H

P

P

A

K

V

M

L

L

A

E

-

Y

A

A

V

A

K

A

E

K

V

L

V

K

E

E

E

A

A

Q

K

K

G

R

S

G

L

V

L

I

D

D

A

Y

Y

F

V

V

F

Y

H

N

I

V

G

G

D
|
D

I

I

V

S

L

L

L

M

S

T

H

H

T

T

Q

K

G

G

V

E

A

D

H

N

P

K

A

D

I

I

H

H

E

G

L

L

A

A

W

W

K

E

A

T

F

F

R

K

E

E

G

V

T

T

-

D

E

Q

V

I

A

A

K

K

R

R

E

F

G

K

L

L

Y
|
Y

G

G

A

A

G

G

Q
|
Q

D

D

L

L

K

K

D

D

A

A

F

F

T

S

G
|
G

N
|
N

L

I

H

R

G

G

L

M

G

G

P

P

Q

Q

V

V

A

A

E

E

M

M

E

E

F

F

A

E

E

E

R

R

P

P

S

S

E

E

P

P

F

I

M

I

V

A

L

F

A

A

D
|
D

K
|
K

T

T

E

E

P

P

G

G

A

A

F

F

N

N

L

L

P

P

L

L

Y

Y

L

K

A

M

F

F

A

A

D

D

P

P

M

F

Y

T

S

T

S

A

G

G

L

L

L

V

L

I

S

D

P

P

E

S

L

M

R

H

P

E

G

G

F

F

R

I

F

F

R

E

I

V

M

L

D

D

L

V

A

-

Q

-

T

V

E

E

R

H

D

K

S

V

Y

Y

I

L

E

-

L

L

D

K

A

T

P

P

E

E

R

D

L

A

Y

Y

D

S

I

L

A

L

A

G

L

L

L

I

R

G

D

T

S

T

H

G

R

R

F

Y

A

I

I

I

A

R

S

K

I

V

W

F

L

R

R

R

K

A

Y

D

G

G

E

A

V

P

A

A

V

A

V

N

S

S

T

V

T

E

R

R

L

L

R

S

N

L

I

I

A

A

G

G

R

R

Y
|
Y

V

V

G

G

K
|
K

D
|
D

P

P

V

V

A

L

L

L

V

V

R

R

T

A

Q
|
Q

K
x
S

I

G

F

L

P

P

A

A

T

V

E

G

E

E

F

V

G

L

P

E

P

A

F

F

A

A

L

H

A

P

P

H

F

L

V

V

A

H

G

G

D

W

T

M

R
|
R

G

G

S

S

H

H

H

A

L

G

P

P

L

L

M

M

P

P

V

A

K

R

-

F

-

I

-

S

-

V

-

D

-

P

-

E

-

R

-

I

A

A

N

I

T

G

P

P

A

K

S

M

T

T

F

R

F

F

-
x
D

C

G

V

P

P

P

M

K

V

V

C

G

A

A

L

L

G

G

F

F

S

Q

L

L

K

H

E

E

G

G

R

Y

L

L

T

E

G

G

P

G

V

V

D

D

L

L

F

F

A

D

D

D

P

P

V

A

W

F

D

D

A

Y

V

V

R

R

A

Q

K

T

V

A

E

Q

K

I

A

A

Q

D

E

Y

M

I

R

R

Q

M

G

G

F

P

Y

F

G

Q

P

P

A

H

M

R

L

L

P

P

M

P

E

E

L

M

E

E

Y
|
Y

T

T

G

A

I

L

A

P

E

K

R

I

L

L

K

A

E

K

L

V

E

K

D11 (= D11) binding Mg(2+)
H18 (= H18) binding in other chain; binding dihydroxyacetone phosphate; binding Mg(2+)
D52 (= D51) binding Mg(2+); binding Mg(2+)
D53 (= D52) binding Mg(2+)
Y91 (= Y89) binding in other chain
Q95 (= Q93) binding Mg(2+)
GN 104:105 (= GN 102:103) binding in other chain
D132 (= D130) binding Mg(2+)
K133 (= K131) binding in other chain; binding dihydroxyacetone phosphate
Y229 (= Y230) mutation to F: Shows unaltered FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
K232 (= K233) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity
D233 (= D234) binding Mg(2+); binding Mg(2+)
D234 (= D235) binding Mg(2+); binding Mg(2+)
QS 242:243 (≠ QK 243:244) binding beta-D-fructose 1,6-bisphosphate
R266 (= R267) binding in other chain; binding dihydroxyacetone phosphate
D297 (vs. gap) binding in other chain; binding dihydroxyacetone phosphate; mutation to N: 18-fold decrease in FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
Y358 (= Y348) binding in other chain

1umgA Crystal structure of fructose-1,6-bisphosphatase (see paper)
46% identity, 100% coverage: 2:363/363 of query aligns to 1:358/359 of 1umgA

query
sites
1umgA

R

K

I

T

T

T

L

I

S

S

V

V

L

I

K

K

A

A

D
|
D

I

I

G

G

S

S

V

L

G

A

G

G

H
|
H

T

H

L

I

P

V

S

H

P

P

A

D

V

T

L

M

A

A

V

A

K

N

E

K

V

V

V

L

E

A

E

S

A

A

K

K

-

E

G

Q

S

G

L

I

L

L

D

D

A

Y

Y

Y

V

I

F

T

H

H

I

V

G

G

D
|
D

I

L

V

Q

L

L

L

I

L

M

S

T

H

H

T

T

Q

R

G

G

V

E

A

L

H

D

P

T

A

K

I

V

H

H

E

E

L

T

A

A

W

W

K

N

A

A

F

F

R

K

E

E

G

A

T

A

E

K

V

V

A

A

K

K

R

D

E

L

G

G

L

L

Y
|
Y

G

A

A

A

G

G

Q
|
Q

D

D

L

L

K

S

D

D

A

S

F

F

T
x
S

G
|
G

N
|
N

L

V

H

R

G

G

L

L

G

G

P

P

Q

G

V

V

A

A

E

E

M

M

E

E

F

I

A

E

E

E

R

R

P

A

S

S

E

E

P

P

F

I

M

A

V

I

L

F

A

M

A

A

D
|
D

K
|
K

T

T

E

E

P

P

G

G

A

A

F

Y

N

N

L

L

P

P

L

L

Y

Y

L

K

A

M

F

F

A

A

D

D

P

P

M

F

Y

N

S

T

S

P

G

G

L

L

L

V

L

I

S

D

P

P

E

T

L

M

R

H

P

G

G

G

F

F

R

K

F

F

R

E

I

V

M

L

D

D

L

V

A

Y

Q

Q

T

G

E

E

R

A

D

-

S

-

Y

-

I

V

E

M

L

L

D

S

A

A

P

P

E

Q

R

E

L

I

Y

Y

D

D

I

L

A

L

A

A

L

L

L

I

R

G

D

T

S

P

H

A

R

R

F

Y

A

V

I

I

A

R

S

R

I

V

W

Y

L

R

R

N

K

E

Y

D

G

N

E

L

V

L

A

A

V

V

S

S

T

I

T

E

R

R

L

L

R

N

N

L

I

I

A

-

G

-

R

-

Y

Y

V

V

G

G

K

K

D
|
D

P

P

V

V

A

M

L

I

V

V

R

R

T

L

Q

Q

K

H

I

G

F

L

P

P

A

A

T

L

E

G

E

E

F

A

G

L

P

E

P

A

F

F

A

A

L

F

A

P

P

H

F

L

V

V

A

P

G

G

D

W

T
x
M

R
|
R

G

G

S

S

H

H

H

Y

L

G

P

P

L

L

M

M

P

P

V

V

-

S

K

Q

A

R

N

D

T

A

P

K

A

A

S

T

T

R

F

F

F
x
D

C

G

V

P

P

P

M

R

V

L

C

L

A

G

L

L

G

G

F

F

S

N

L

V

K

K

E

N

G

G

R

R

L

L

T

V

G

G

P

P

V

T

D

D

L

L

F

F

A

D

D

D

P

P

V

A

W

F

D

D

A

E

V

T

R

R

A

R

K

L

V

A

V

N

E

I

K

V

A

A

Q

D

E

Y

M

M

R

R

Q

H

G

G

F

P

Y

F

G

M

P

P

A

H

M

R

L

L

P

E

M

P

E

T

E

E

L

M

E

E

Y
|
Y

T

T

G

T

I

L

A

P

E

L

R

I

L

L

K

E

E

K

L

L

E

K

R

D

E

R

F

F

S

K

binding 1,6-fructose diphosphate (linear form): H17 (= H18), D51 (= D51), Y89 (= Y89), Q93 (= Q93), S101 (≠ T101), G102 (= G102), N103 (= N103), K131 (= K131), D228 (= D234), D229 (= D235), M260 (≠ T266), R261 (= R267), D282 (≠ F287), Y343 (= Y348)
binding magnesium ion: D10 (= D11), H17 (= H18), D51 (= D51), D51 (= D51), D52 (= D52), Q93 (= Q93), D130 (= D130), D228 (= D234), D229 (= D235), D229 (= D235)

3t2eA Fructose-1,6-bisphosphate aldolase/phosphatase from thermoproteus neutrophilus, f6p-bound form (see paper)
47% identity, 99% coverage: 1:359/363 of query aligns to 1:365/385 of 3t2eA

query
sites
3t2eA

M

M

R

R

I

V

T

T

L

V

S

S

V

I

L

I

K

K

A

A

D
|
D

I

V

G

G

S

G

V

F

G

P

G

G

H
|
H

T

A

L

H

P

V

S

H

P

P

A

K

V

M

L

L

A

E

-

Y

A

A

V

A

K

A

E

K

V

L

V

K

E

E

E

A

A

Q

K

K

G

R

S

G

L

V

L

I

D

D

A

Y

Y

F

V

V

F

Y

H

N

I

V

G

G

D
|
D

I

I

V

S

L

L

L

M

S

T

H

H

T

T

Q

K

G

G

V

E

A

D

H

N

P

K

A

D

I

I

H

H

E

G

L

L

A

A

W

W

K

E

A

T

F

F

R

K

E

E

G

V

T

T

-

D

E

Q

V

I

A

A

K

K

R

R

E

F

G

K

L

L

Y
|
Y

G

G

A

A

G

G

Q
|
Q

D

D

L

L

K

K

D

D

A

A

F

F

T

S

G

G

N

N

L

I

H

R

G

G

L

M

G

G

P

P

Q

Q

V

V

A

A

E

E

M

M

E

E

F

F

A

E

E

E

R

R

P

P

S

S

E

E

P

P

F

I

M

I

V

A

L

F

A

A

D
|
D

K

K

T

T

E

E

P

P

G

G

A

A

F

F

N

N

L

L

P

P

L

L

Y

Y

L

K

A

M

F

F

A

A

D

D

P

P

M

F

Y

T

S

T

S

A

G

G

L

L

L

V

L

I

S

D

P

P

E

S

L

M

R

H

P

E

G

G

F

F

R

I

F

F

R

E

I

V

M

L

D

D

L

V

A

-

Q

-

T

V

E

E

R

H

D

K

S

V

Y

Y

I

L

E

-

L

L

D

K

A

T

P

P

E

E

R

D

L

A

Y

Y

D

S

I

L

A

L

A

G

L

L

L

I

R

G

D

T

S

T

H

G

R

R

F

Y

A

I

I

I

A

R

S

K

I

V

W

F

L

R

R

R

K

A

Y

D

G

G

E

A

V

P

A

A

V

A

V

N

S

S

T

V

T

E

R

R

L

L

R

-

N

-

I

-

A

-

G

S

R

L

Y

Y

V

V

G

G

K

K

D

D

D
|
D

P

P

V

V

A

L

L

L

V

V

R

R

T

A

Q

Q

K

S

I

G

F

L

P

P

A

A

T

V

E

G

E

E

F

V

G

L

P

E

P

A

F

F

A

A

L

H

A

P

P

H

F

L

V

V

A

H

G

G

D

W

T
x
M

R
|
R

G

G

S

S

H

H

H

A

L

G

P

P

L

L

M

M

P

P

V

A

K

R

-

F

-

I

-

S

-

V

-

D

-

P

-

E

-

R

-

I

A

A

N

I

T

G

P

P

A

K

S

M

T

T

F

R

F

F

-
x
D

C

G

V

P

P

P

M

K

V

V

C

G

A

A

L

L

G

G

F

F

S

Q

L

L

K

H

E

E

G

G

R

Y

L

L

T

E

G

G

P

G

V

V

D

D

L

L

F

F

A

D

D

D

P

P

V

A

W

F

D

D

A

Y

V

V

R

R

A

Q

K

T

V

A

E

Q

K

I

A

A

Q

D

E

Y

M

I

R

R

Q

M

G

G

F

P

Y

F

G

Q

P

P

A

H

M

R

L

L

P

P

M

P

E

E

L

M

E

E

Y
|
Y

T

T

G

A

I

L

A

P

E

K

R

I

L

L

K

A

E

K

L

V

E

K

binding fructose -6-phosphate: H18 (= H18), Y91 (= Y89), M261 (≠ T266), R262 (= R267), D293 (vs. gap), Y354 (= Y348)
binding magnesium ion: D11 (= D11), H18 (= H18), D52 (= D51), D52 (= D51), D53 (= D52), Q95 (= Q93), D132 (= D130), D230 (= D235)

Query Sequence

>WP_053768266.1 NCBI__GCF_001280255.1:WP_053768266.1
MRITLSVLKADIGSVGGHTLPSPAVLAAVKEVVEEAKGSLLLDAYVFHIGDDIVLLLSHT
QGVAHPAIHELAWKAFREGTEVAKREGLYGAGQDLLKDAFTGNLHGLGPQVAEMEFAERP
SEPFMVLAADKTEPGAFNLPLYLAFADPMYSSGLLLSPELRPGFRFRIMDLAQTERDSYI
ELDAPERLYDIAALLRDSHRFAIASIWLRKYGEVAAVVSTTRLRNIAGRYVGKDDPVALV
RTQKIFPATEEFGPPFALAPFVAGDTRGSHHLPLMPVKANTPASTFFCVPMVCALGFSLK
EGRLTGPVDLFADPVWDAVRAKVVEKAQEMRRQGFYGPAMLPMEELEYTGIAERLKELER
EFS

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