SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_041277980.1 NCBI__GCF_000025945.1:WP_041277980.1 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 10 hits to proteins with known functional sites (download)

P58315 Fructose-bisphosphate aldolase class 1; Fructose-bisphosphate aldolase class I; FBP aldolase; FBPA; EC 4.1.2.13 from Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1) (see paper)
30% identity, 92% coverage: 21:302/306 of query aligns to 3:263/263 of P58315

query
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P58315

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W144 (= W176) mutation to E: Loss of FBP aldolase activity; when associated with F-146.
Y146 (= Y178) mutation to F: The catalytic activity is at least 3-fold lower than for the wild-type. Loss of FBP aldolase activity; when associated with E-144.

2yceE Structure of an archaeal fructose-1,6-bisphosphate aldolase with the catalytic lys covalently bound to the carbinolamine intermediate of the substrate. (see paper)
30% identity, 90% coverage: 21:296/306 of query aligns to 1:255/255 of 2yceE

query
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2yceE

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binding d-mannitol-1,6-diphosphate: D22 (= D42), H23 (≠ Q43), H27 (= H47), W142 (= W176), R146 (= R180), K175 (= K209), K177 (≠ N211), G201 (= G240), G202 (= G241), V228 (≠ T267), G229 (= G268), R230 (= R269)

1w8sA The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates (see paper)
31% identity, 87% coverage: 21:287/306 of query aligns to 1:250/250 of 1w8sA

query
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1w8sA

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binding 1,6-di-O-phosphono-beta-D-fructofuranose: A20 (= A40), D22 (= D42), H23 (≠ Q43), H27 (= H47), R146 (= R180), K175 (= K209), K177 (≠ N211), S200 (≠ A239), G201 (= G240), G202 (= G241), V228 (≠ T267), G229 (= G268), R230 (= R269)

P58314 Fructose-bisphosphate aldolase class 1; Fructose-bisphosphate aldolase class I; FBP aldolase; EC 4.1.2.13 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see paper)
32% identity, 88% coverage: 34:301/306 of query aligns to 21:276/281 of P58314

query
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P58314

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K191 (= K209) mutation to A: Loss of activity.

P0A991 Fructose-bisphosphate aldolase class 1; Fructose-bisphosphate aldolase class I; FBP aldolase; EC 4.1.2.13 from Escherichia coli (strain K12) (see 2 papers)
26% identity, 85% coverage: 34:294/306 of query aligns to 66:346/350 of P0A991

query
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P0A991

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Y

Y

L

F

G

G

S

S

E

E

Y

E

E

S

P

R

E

R

M

Q

L

I

H

E

Q

E

A

I

A

S

Q

A

I

A

I

F

S

E

H

R

A

A

H

H

Q

E

H

L

G

G

L

M

I

V

S

T

V

V

L

L

W

W

V

A

Y

Y

P

L

R

R

G

N

K

S

A

A

V

F

-
x
K

A

K

D

D

E

G

K

V

D

D

P

Y

H

H

L

V

I

S

A

A

G

D

A

L

T

T

G

G

A

Q

-

A

-

N

-

H

-

L

A

A

C

T

L

I

G

G

S

A

D

D

F

I

V

V

K
|
K

-

Q

-
x
K

-

M

-

A

-

E

-

N

-

G

-

Y

-

K

-

A

V

I

N

N

Y

Y

P

G

K

Y

K

T

E

D

D

D

C

R

A

V

S

Y

K

S

E
x
K

I

L

F

T

K

S

E

E

-

N

-

P

-

I

-

D

-

L

-

V

-

R

-

Y

-

Q

-

L

A

A

V

N

M

C

A

Y

A

M

G

G

R

R

T

A

K

G

V

L

V

I

C

N

A

S

G

G

S

A

D

-

V

-

E

-

G

G

F

G

L

E

E

T

R

D

L

L

Y

S

D

D

Q

A

I

V

H

R

V

T

-

A

-

V

-

I

-

N

-

K

-

R

S

A

G

G

A

G

S

M

G

G

N

L

A

I

T

L

G

G

R

R

N

K

I

A

H

F

Q

K

K

K

A

S

L

M

K

A

E

D

A

G

I

V

R

K

M

L

C

I

N

N

A

A

I

V

Y

Q

A

D

I

V

T

Y

V

L

D

D

G

S

K

K

K208 (vs. gap) modified: N6-acetyllysine
K237 (= K209) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to A: Loss of activity.
K239 (vs. gap) mutation to A: No change in activity.
K262 (≠ E222) modified: N6-acetyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2qjgA M. Jannaschii adh synthase complexed with f1,6p (see paper)
31% identity, 53% coverage: 140:301/306 of query aligns to 115:268/272 of 2qjgA

query
sites
2qjgA

A

A

V

V

G

S

Y

I

T

H

V

V

Y

N

L

V

G

G

S

S

E

D

Y

E

E

D

P

W

E

E

M

A

L

Y

H

R

Q

D

A

L

A

G

Q

M

I

I

I

A

S

E

H

T

A

C

H

E

Q

Y

H

W

G

G

L

M

I

P

S

L

V

I

L

A

W

M

V

M

Y
|
Y

P

P

R
|
R

G

G

K

K

A

H

V

I

A

Q

D

N

E

E

K

R

D

D

P

P

H

E

L

L

I

V

A

A

G

H

A

A

T

A

G

R

A

L

A

G

A

A

C

E

L

L

G

G

S

A

D

D

F

I

V

V

K
|
K

V

T

N

S

Y

Y

P

T

K

G

K

D

E

I

D

D

C

S

A

-

S

-

K

-

E

-

I

-

F

F

K

R

E

D

A

V

V

V

M

K

A

G

A

C

G

P

R

A

T

P

K

V

V

V

C

A

A
x
G

G
|
G

G

P

S

K

S

T

D

N

D

T

V

D

E

E

G

E

F

F

L

L

E

Q

R

M

L

I

Y

K

D

D

Q

A

I

M

H

E

V

-

S

A

G

G

A

A

S

A

G

G

N

V

A

A

T
x
V

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

H

A

-

L

-

K

D

E

D

A

V

I

V

R

G

M

I

C

T

N

R

A

A

I

V

Y

C

A

K

I

I

T

V

V

H

D

E

G

N

K

A

T

D

V

V

N

E

E

E

A

A

M

L

K

K

binding 1,6-di-o-phosphono-d-allitol: Y153 (= Y178), R155 (= R180), K184 (= K209), G209 (≠ A239), G210 (= G240), V236 (≠ T267), G237 (= G268), R238 (= R269)

Sites not aligning to the query:

binding 1,6-di-o-phosphono-d-allitol: 34, 37

P76143 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase; EC 2.3.1.245 from Escherichia coli (strain K12) (see paper)
29% identity, 55% coverage: 136:303/306 of query aligns to 133:286/291 of P76143

query
sites
P76143

L

L

N

N

I

S

L

C

A

A

V

V

G

A

Y

A

T

Q

V

V

Y

Y

L

I

G

G

S

S

E

E

Y

Y

E

E

P

H

E

Q

M

S

L

I

H

K

Q

N

A

I

Q

Q

I

L

I

V

S

D

H

A

A

G

H

M

Q

K

H

V

G

G

L

M

I

-

S

P

V

T

L

M

W

A

V

V

Y

T

P

G

R

V

G

G

K

K

A

D

V

M

A

V

D

-

E

-

K

R

D

D

P

Q

H

R

L

Y

I

F

A

S

G

L

A

A

T

T

G

R

A

I

A

A

C

E

L

M

G

G

S

A

D

Q

F

I

V

I

K
|
K

V

T

N

Y

Y

Y

P

V

K

E

K

K

E

G

D

-

C

-

A

-

S

-

K

-

E

-

I

-

F

-

K

F

E

E

A

R

V

I

M

V

A

A

A

G

G

C

R

P

T

V

K

P

V

I

V

V

C

I

A

A

G

G

S

K

D

L

D

P

V

E

E

R

G

E

F

A

L

L

E

E

R

M

L

C

Y

W

D

Q

Q

A

I

I

H

D

V

-

S

Q

G

G

A

A

S

S

G

G

N

V

A
x
D

T

M

G

G

R

R

N

N

I

I

H

F

Q

Q

K

S

A

-

L

-

K

D

E

H

A

P

I

V

R

A

M

M

C

M

N

K

A

A

I

V

Y

Q

A

A

I

V

T

V

V

H

D

H

G

N

K

E

T

T

V

A

N

D

E

R

A

A

M

Y

K

E

I

L

Y

Y

K203 (= K209) active site, Schiff-base intermediate with substrate; mutation to A: No activity.
D251 (≠ A266) mutation to A: No activity.

Sites not aligning to the query:

57 D→A: No activity.

3gndA Crystal structure of e. Coli lsrf in complex with ribulose-5-phosphate (see paper)
28% identity, 55% coverage: 136:303/306 of query aligns to 124:273/276 of 3gndA

query
sites
3gndA

L

L

N

N

I

S

L

C

A

A

V

V

G

A

Y

A

T

Q

V

V

Y

Y

L

I

G

G

S

S

E

E

Y

Y

E

E

P

H

E

Q

M

S

L

I

H

K

Q

N

A

I

Q

Q

I

L

I

V

S

D

H

A

A

G

H

M

Q

K

H

V

G

G

L

M

I

-

S

-

V

-

L

-

W

-

V

-

Y

-

P

P

R

T

G

M

K

A

A

V

V

T

A

G

D

V

E

V

K

R

D

D

P

Q

H

R

L

Y

I

F

A

S

G

L

A

A

T

T

G

R

A

I

A

A

C

E

L

M

G

G

S

A

D

Q

F

I

V

I

K
|
K

V

T

N

Y

Y

Y

P

V

K

E

K

K

E

G

D

-

C

-

A

-

S

-

K

-

E

-

I

-

F

-

K

F

E

E

A

R

V

I

M

V

A

A

A

G

G

C

R

P

T

V

K

P

V

I

V

V

C

I

A

A

G
|
G

S

K

D

L

D

P

V

E

E

R

G

E

F

A

L

L

E

E

R

M

L

C

Y

W

D

Q

Q

A

I

I

H

D

V

-

S

Q

G

G

A

A

S

S

G

G

N

V

A
x
D

T
x
M

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

S

A

-

L

-

K

D

E

H

A

P

I

V

R

A

M

M

C

M

N

K

A

A

I

V

Y

Q

A

A

I

V

T

V

V

H

D

H

G

N

K

E

T

T

V

A

N

D

E

R

A

A

M

Y

K

E

I

L

Y

Y

binding ribulose-5-phosphate: K190 (= K209), G213 (= G240), G214 (= G241), D238 (≠ A266), M239 (≠ T267), G240 (= G268), R241 (= R269)

Sites not aligning to the query:

binding ribulose-5-phosphate: 48, 49, 51

3glcA Crystal structure of e. Coli lsrf in complex with ribose-5-phosphate (see paper)
28% identity, 55% coverage: 136:303/306 of query aligns to 124:273/276 of 3glcA

query
sites
3glcA

L

L

N

N

I

S

L

C

A

A

V

V

G

A

Y

A

T

Q

V

V

Y

Y

L

I

G

G

S

S

E

E

Y

Y

E

E

P

H

E

Q

M

S

L

I

H

K

Q

N

A

I

Q

Q

I

L

I

V

S

D

H

A

A

G

H

M

Q

K

H

V

G

G

L

M

I

-

S

-

V

-

L

-

W

-

V

-

Y

-

P

P

R

T

G

M

K

A

A

V

V

T

A

G

D

V

E

V

K

R

D

D

P

Q

H

R

L

Y

I

F

A

S

G

L

A

A

T

T

G

R

A

I

A

A

C

E

L

M

G

G

S

A

D

Q

F

I

V

I

K
|
K

V

T

N

Y

Y

Y

P

V

K

E

K

K

E

G

D

-

C

-

A

-

S

-

K

-

E

-

I

-

F

-

K

F

E

E

A

R

V

I

M

V

A

A

A

G

G

C

R

P

T

V

K

P

V

I

V

V

C

I

A

A

G
|
G

S

K

D

L

D

P

V

E

E

R

G

E

F

A

L

L

E

E

R

M

L

C

Y

W

D

Q

Q

A

I

I

H

D

V

-

S

Q

G

G

A

A

S

S

G

G

N

V

A

D

T

M

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

S

A

-

L

-

K

D

E

H

A

P

I

V

R

A

M

M

C

M

N

K

A

A

I

V

Y

Q

A

A

I

V

T

V

V

H

D

H

G

N

K

E

T

T

V

A

N

D

E

R

A

A

M

Y

K

E

I

L

Y

Y

binding ribose-5-phosphate: K190 (= K209), G213 (= G240), G214 (= G241), G240 (= G268), R241 (= R269)

Sites not aligning to the query:

binding ribose-5-phosphate: 48, 49

4p2vA Structure of the ai-2 processing enzyme lsrf in complex with the product of the lsrg reaction p-hpd (see paper)
29% identity, 55% coverage: 136:303/306 of query aligns to 125:278/281 of 4p2vA

query
sites
4p2vA

L

L

N

N

I

S

L

C

A

A

V

V

G

A

Y

A

T

Q

V

V

Y

Y

L

I

G

G

S

S

E

E

Y

Y

E

E

P

H

E

Q

M

S

L

I

H

K

Q

N

A

I

Q

Q

I

L

I

V

S

D

H

A

A

G

H

M

Q

K

H

V

G

G

L

M

I

-

S

P

V

T

L

M

W

A

V

V

Y

T

P

G

R

V

G

G

K

K

A

D

V

M

A

V

D

-

E

-

K

R

D

D

P

Q

H

R

L

Y

I

F

A

S

G

L

A

A

T

T

G

R

A

I

A

A

C

E

L

M

G

G

S

A

D

Q

F

I

V

I

K

A

V

T

N
x
Y

Y

Y

P

V

K

E

K

K

E

G

D

-

C

-

A

-

S

-

K

-

E

-

I

-

F

-

K

F

E

E

A

R

V

I

M

V

A

A

A

G

G

C

R

P

T

V

K

P

V

I

V

V

C

I

A

A

G
|
G

S

K

D

L

D

P

V

E

E

R

G

E

F

A

L

L

E

E

R

M

L

C

Y

W

D

Q

Q

A

I

I

H

D

V

-

S

Q

G

G

A

A

S

S

G

G

N

V

A

D

T

M

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

S

A

-

L

-

K

D

E

H

A

P

I

V

R

A

M

M

C

M

N

K

A

A

I

V

Y

Q

A

A

I

V

T

V

V

H

D

H

G

N

K

E

T

T

V

A

N

D

E

R

A

A

M

Y

K

E

I

L

Y

Y

binding (3R)-3-hydroxy-2,4-dioxopentyl dihydrogen phosphate: Y197 (≠ N211), G218 (= G240), G219 (= G241), G245 (= G268), R246 (= R269)

Sites not aligning to the query:

binding (3R)-3-hydroxy-2,4-dioxopentyl dihydrogen phosphate: 50

Query Sequence

>WP_041277980.1 NCBI__GCF_000025945.1:WP_041277980.1
MNLKEDDILVPLDVPKAERENYIHNYLAITQNCGRLMLFAGDQKVEHLNSDFYGEGIHPD
DGNPEHLFRIASQANIGVFATQLGLIARYGSSYADVPYLVKLNSRTNLVKTSQSDPFSNQ
WLDVQQVVDFRKNSGLNILAVGYTVYLGSEYEPEMLHQAAQIISHAHQHGLISVLWVYPR
GKAVADEKDPHLIAGATGAAACLGSDFVKVNYPKKEDCASKEIFKEAVMAAGRTKVVCAG
GSSDDVEGFLERLYDQIHVSGASGNATGRNIHQKALKEAIRMCNAIYAITVDGKTVNEAM
KIYTAA

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