SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_015411299.1 NCBI__GCF_000007065.1:WP_015411299.1 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)
33% identity, 82% coverage: 25:275/307 of query aligns to 6:237/263 of P58315

query
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P58315

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W144 (= W177) mutation to E: Loss of FBP aldolase activity; when associated with F-146.
Y146 (= Y179) 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)
32% identity, 86% coverage: 25:287/307 of query aligns to 4:245/255 of 2yceE

query
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2yceE

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binding d-mannitol-1,6-diphosphate: D22 (= D43), H23 (≠ Q44), H27 (= H48), W142 (= W177), R146 (= R181), K175 (= K210), K177 (≠ N212), G201 (= G241), G202 (= G242), V228 (≠ T268), G229 (= G269), R230 (= R270)

1w8sA The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates (see paper)
32% identity, 82% coverage: 25:275/307 of query aligns to 4:235/250 of 1w8sA

query
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1w8sA

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binding 1,6-di-O-phosphono-beta-D-fructofuranose: A20 (= A41), D22 (= D43), H23 (≠ Q44), H27 (= H48), R146 (= R181), K175 (= K210), K177 (≠ N212), S200 (≠ A240), G201 (= G241), G202 (= G242), V228 (≠ T268), G229 (= G269), R230 (= R270)

2qjgA M. Jannaschii adh synthase complexed with f1,6p (see paper)
34% identity, 52% coverage: 142:302/307 of query aligns to 116:268/272 of 2qjgA

query
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2qjgA

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binding 1,6-di-o-phosphono-d-allitol: Y153 (= Y179), R155 (= R181), K184 (= K210), G209 (≠ A240), G210 (= G241), V236 (≠ T268), G237 (= G269), R238 (= R270)

Sites not aligning to the query:

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

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)
27% identity, 83% coverage: 34:287/307 of query aligns to 65:338/350 of P0A991

query
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P0A991

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R

R

N

K

I

A

H

F

Q

K

K

K

P

S

L

M

D

A

E

D

A

G

V

V

R

K

M

L

C

I

N

N

A

A

V

V

K208 (vs. gap) modified: N6-acetyllysine
K237 (= K210) 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 (≠ E223) modified: N6-acetyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

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)
29% identity, 79% coverage: 35:275/307 of query aligns to 21:251/281 of P58314

query
sites
P58314

G

G

K

R

L

A

M

L

L

I

F

F

A

A

G

M

D

D

Q

H

K

G

V

F

E

E

H

H

L

G

N

P

D

T

D

D

F

F

F

-

G

-

P

-

E

E

V

P

P

V

E

W

D

E

D

H

A

V

D

N

P

P

E

R

H

V

L

I

F

I

R

R

I

K

A

V

Q

R

S

A

K

G

I

I

G

D

V

G

F

V

A

M

T

M

Q

L

L

P

G

G

L

L

I

A

A

R

R

I

Y

A

G

G

M

D

D

E

Y

V

K

K

-

P

D

E

I

V

P

G

Y

L

L

M

V

I

K

K

V

L

N

T

S

S

K

K

T

T

N

N

L

L

V

R

E

P

T

K

E

P

Q

E

A

Q

D

L

P

L

F

Q

S

S

N

Q

L

L

W

G

Y

F

D

V

I

D

D

D

Q

A

V

I

A

K

E

-

F

-

R

-

E

-

N

-

S

-

G

-

L

L

N

G

I

A

L

D

G

A

V

I

G

A

Y

A

T

T

I

V

Y

Y

L

W

G

G

S

S

E

P

F

Q

E

E

A

D

E

V

M

M

L

M

V

R

Q

Q

A

F

A

A

Q

E

V

I

V

V

Y

S

D

Y

A

A

H

H

Q

D

H

L

G

G

M

Y

L

P

S

V

V

V

L

Q

W

F

I

A

Y

Y

P

P

R

R

G

G

A

P

A

Y

V

I

K

-

D

D

E

E

K

K

-

Y

-

G

-

K

-

E

D

D

P

Y

H

R

L

V

I

V

A

M

G

Y

A

G

T

A

G

R

V

A

G

A

A

A

C

E

L

S

G

G

S

A

D

D

F

M

V

I

K
|
K

V

T

N

Y

Y

W

P

-

K

-

E

-

G

-

E

T

K

G

S

S

A

K

E

E

I

T

F

F

K

A

E

K

A

V

V

V

K

E

A

A

G

A

R

G

T

V

K

P

V

V

V

L

C

L

A

S

G

G

S

A

S

K

D

T

E

E

A

N

E

P

A

V

-

D

F

F

L

L

K

K

K

V

L

V

H

W

D

E

Q

V

I

I

H

E

I

A

S

G

G

G

A

A

Q

-

G

G

N

A

A

V

T

V

G

G

R

R

N

N

I

I

H

F

Q

Q

K

R

K191 (= K210) mutation to A: Loss of activity.

3gndA Crystal structure of e. Coli lsrf in complex with ribulose-5-phosphate (see paper)
27% identity, 56% coverage: 137:307/307 of query aligns to 124:276/276 of 3gndA

query
sites
3gndA

L

L

N

N

I

S

L

C

G

A

V

V

G

A

Y

A

T

Q

I

V

Y

Y

L

I

G

G

S

S

E

E

F

Y

E

E

A

H

E

Q

M

S

L

I

V

K

Q

N

A

I

Q

Q

V

L

V

V

Y

D

D

A

A

G

H

M

Q

K

H

V

G

G

M

M

L

-

S

-

V

-

L

-

W

-

I

-

Y

-

P

P

R

T

G

M

A

A

A

V

V

T

K

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

V

I

G

A

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

G

F

E

E

K

R

S

-

A

-

E

-

I

-

F

-

K

-

E

-

A

-

V

I

K

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

E

P

A

E

E

R

A

E

F

A

L

L

K

E

K

M

L

C

H

W

D

Q

Q

A

I

I

H

D

I

-

S

Q

G

G

A

A

Q

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

P

-

L

-

D

D

E

H

A

P

V

V

R

A

M

M

C

M

N

K

A

A

V

V

Y

Q

A

A

I

V

T

V

V

H

E

H

D

N

A

E

S

T

V

A

E

D

D

R

A

A

L

Y

R

E

I

L

Y

Y

S

L

G

S

E

E

binding ribulose-5-phosphate: K190 (= K210), G213 (= G241), G214 (= G242), D238 (≠ A267), M239 (≠ T268), G240 (= G269), R241 (= R270)

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)
27% identity, 56% coverage: 137:307/307 of query aligns to 124:276/276 of 3glcA

query
sites
3glcA

L

L

N

N

I

S

L

C

G

A

V

V

G

A

Y

A

T

Q

I

V

Y

Y

L

I

G

G

S

S

E

E

F

Y

E

E

A

H

E

Q

M

S

L

I

V

K

Q

N

A

I

Q

Q

V

L

V

V

Y

D

D

A

A

G

H

M

Q

K

H

V

G

G

M

M

L

-

S

-

V

-

L

-

W

-

I

-

Y

-

P

P

R

T

G

M

A

A

A

V

V

T

K

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

V

I

G

A

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

G

F

E

E

K

R

S

-

A

-

E

-

I

-

F

-

K

-

E

-

A

-

V

I

K

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

E

P

A

E

E

R

A

E

F

A

L

L

K

E

K

M

L

C

H

W

D

Q

Q

A

I

I

H

D

I

-

S

Q

G

G

A

A

Q

S

G

G

N

V

A

D

T

M

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

S

P

-

L

-

D

D

E

H

A

P

V

V

R

A

M

M

C

M

N

K

A

A

V

V

Y

Q

A

A

I

V

T

V

V

H

E

H

D

N

A

E

S

T

V

A

E

D

D

R

A

A

L

Y

R

E

I

L

Y

Y

S

L

G

S

E

E

binding ribose-5-phosphate: K190 (= K210), G213 (= G241), G214 (= G242), G240 (= G269), R241 (= R270)

Sites not aligning to the query:

binding ribose-5-phosphate: 48, 49

P76143 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase; EC 2.3.1.245 from Escherichia coli (strain K12) (see paper)
27% identity, 56% coverage: 137:307/307 of query aligns to 133:289/291 of P76143

query
sites
P76143

L

L

N

N

I

S

L

C

G

A

V

V

G

A

Y

A

T

Q

I

V

Y

Y

L

I

G

G

S

S

E

E

F

Y

E

E

A

H

E

Q

M

S

L

I

V

K

Q

N

A

I

Q

Q

V

L

V

V

Y

D

D

A

A

G

H

M

Q

K

H

V

G

G

M

M

L

P

S

T

V

M

L

A

W

V

I

T

Y

G

P

V

R

G

G

K

A

D

A

M

V

V

K

R

D

D

E

Q

K

R

D

Y

P

F

H

S

L

L

I

-

A

-

G

-

A

A

T

T

G

R

V

I

G

A

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

G

F

E

E

K

R

S

-

A

-

E

-

I

-

F

-

K

-

E

-

A

-

V

I

K

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

E

P

A

E

E

R

A

E

F

A

L

L

K

E

K

M

L

C

H

W

D

Q

Q

A

I

I

H

D

I

-

S

Q

G

G

A

A

Q

S

G

G

N

V

A
x
D

T

M

G

G

R

R

N

N

I

I

H

F

Q

Q

K

S

P

-

L

-

D

D

E

H

A

P

V

V

R

A

M

M

C

M

N

K

A

A

V

V

Y

Q

A

A

I

V

T

V

V

H

E

H

D

N

A

E

S

T

V

A

E

D

D

R

A

A

L

Y

R

E

I

L

Y

Y

S

L

G

S

E

E

K203 (= K210) active site, Schiff-base intermediate with substrate; mutation to A: No activity.
D251 (≠ A267) mutation to A: No activity.

Sites not aligning to the query:

57 D→A: No activity.

4p2vA Structure of the ai-2 processing enzyme lsrf in complex with the product of the lsrg reaction p-hpd (see paper)
27% identity, 56% coverage: 137:307/307 of query aligns to 125:281/281 of 4p2vA

query
sites
4p2vA

L

L

N

N

I

S

L

C

G

A

V

V

G

A

Y

A

T

Q

I

V

Y

Y

L

I

G

G

S

S

E

E

F

Y

E

E

A

H

E

Q

M

S

L

I

V

K

Q

N

A

I

Q

Q

V

L

V

V

Y

D

D

A

A

G

H

M

Q

K

H

V

G

G

M

M

L

P

S

T

V

M

L

A

W

V

I

T

Y

G

P

V

R

G

G

K

A

D

A

M

V

V

K

R

D

D

E

Q

K

R

D

Y

P

F

H

S

L

L

I

-

A

-

G

-

A

A

T

T

G

R

V

I

G

A

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

G

F

E

E

K

R

S

-

A

-

E

-

I

-

F

-

K

-

E

-

A

-

V

I

K

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

E

P

A

E

E

R

A

E

F

A

L

L

K

E

K

M

L

C

H

W

D

Q

Q

A

I

I

H

D

I

-

S

Q

G

G

A

A

Q

S

G

G

N

V

A

D

T

M

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

S

P

-

L

-

D

D

E

H

A

P

V

V

R

A

M

M

C

M

N

K

A

A

V

V

Y

Q

A

A

I

V

T

V

V

H

E

H

D

N

A

E

S

T

V

A

E

D

D

R

A

A

L

Y

R

E

I

L

Y

Y

S

L

G

S

E

E

binding (3R)-3-hydroxy-2,4-dioxopentyl dihydrogen phosphate: Y197 (≠ N212), G218 (= G241), G219 (= G242), G245 (= G269), R246 (= R270)

Sites not aligning to the query:

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

Query Sequence

>WP_015411299.1 NCBI__GCF_000007065.1:WP_015411299.1
MAPIKKEDVTVPLDVPKAMRETYIKNYMEITKESGKLMLFAGDQKVEHLNDDFFGPEVPE
DDADPEHLFRIAAQSKIGVFATQLGLIARYGMDYKDIPYLVKVNSKTNLVETEQADPFSN
LWYDIDQVAEFRENSGLNILGVGYTIYLGSEFEAEMLVQAAQVVYDAHQHGMLSVLWIYP
RGAAVKDEKDPHLIAGATGVGACLGSDFVKVNYPKKEGEKSAEIFKEAVKAAGRTKVVCA
GGSSDEAEAFLKKLHDQIHISGAQGNATGRNIHQKPLDEAVRMCNAVYAITVEDASVEDA
LRIYSGE

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