SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_109967688.1 NCBI__GCF_003173355.1:WP_109967688.1 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)

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)
31% identity, 92% coverage: 20:299/303 of query aligns to 5:263/263 of P58315

query
sites
P58315

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W144 (= W173) mutation to E: Loss of FBP aldolase activity; when associated with F-146.
Y146 (= Y175) 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, 87% coverage: 20:283/303 of query aligns to 3:245/255 of 2yceE

query
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2yceE

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binding d-mannitol-1,6-diphosphate: D22 (= D39), H23 (≠ Q40), H27 (= H44), W142 (= W173), R146 (= R177), K175 (= K206), K177 (≠ E213), G201 (= G237), G202 (= G238), V228 (≠ T264), G229 (= G265), R230 (= R266)

1w8sA The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates (see paper)
32% identity, 87% coverage: 20:283/303 of query aligns to 3:245/250 of 1w8sA

query
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1w8sA

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binding 1,6-di-O-phosphono-beta-D-fructofuranose: A20 (= A37), D22 (= D39), H23 (≠ Q40), H27 (= H44), R146 (= R177), K175 (= K206), K177 (= K211), S200 (≠ A236), G201 (= G237), G202 (= G238), V228 (≠ T264), G229 (= G265), R230 (= R266)

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: 31:298/303 of query aligns to 21:276/281 of P58314

query
sites
P58314

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K191 (= K206) 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)
27% identity, 96% coverage: 8:299/303 of query aligns to 46:349/350 of P0A991

query
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P0A991

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Y

L

F

G

G

S

S

E

E

A

E

E

S

S

R

E

R

M

Q

L

I

S

E

A

E

A

I

A

S

N

A

A

A

I

F

F

E

E

R

A

A

H

H

Q

E

N

L

G

G

L

M

V

V

T

T

V

V

L

L

W

W

I

A

Y

Y

P

L

R

R

G

N

K

S

A

A

V

F

-
x
K

K

K

D

D

E

G

K

V

D

D

P

Y

H

H

L

V

I

S

A

A

G

D

A

L

A

T

G

G

-

Q

-

A

-

N

-

H

V

L

A

A

C

T

L

I

G

G

S

A

D

D

F

I

V

V

K
|
K

V

Q

N
x
K

P

M

P

A

K

E

K

N

E

N

G

G

A

G

-

Y

-

K

-

A

-

I

-

N

-

Y

-

G

-

Y

-

T

-

D

-

R

-

V

-

Y

-

S

-
x
K

-

L

-

T

-

S

-

E

S

N

S

P

V

I

E

D

L

L

M

V

K

R

E

Y

-

Q

-

L

A

A

T

N

L

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

V

-

D

G

G

G

E

E

I

T

F

D

L

L

K

S

Q

D

L

A

W

V

E

R

Q

T

I

A

H

V

I

I

-

N

-

K

-

R

G

A

G

G

C

G

A

M

G

G

N

L

A

I

T

L

G

G

R

R

N

K

I

A

H

F

Q

K

K

K

S

S

L

M

D

A

E

D

A

G

V

V

R

K

M

L

C

I

N

N

A

A

I

-

Y

-

A

-

I

-

T

-

V

V

Q

Q

D

D

A

V

S

Y

I

L

E

D

E

S

A

K

V

I

K

T

I

I

K208 (vs. gap) modified: N6-acetyllysine
K237 (= K206) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to A: Loss of activity.
K239 (≠ N208) mutation to A: No change in activity.
K262 (vs. gap) 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)
29% identity, 53% coverage: 142:302/303 of query aligns to 109:272/272 of 2qjgA

query
sites
2qjgA

I

I

Y

R

L

M

G

G

S

A

E

D

A

A

E

V

S

S

E

I

M

H

L

V

S

N

A

V

A

G

A

S

N

D

A

E

I

D

F

W

E

E

A

A

H

Y

Q

R

N

D

-

L

-

G

-

M

-

I

-

A

-

E

-

T

-

C

-

E

-

Y

-

W

G

G

L

M

V

P

T

L

V

I

L

A

W

M

I

M

Y
|
Y

P

P

R
|
R

G

G

K

K

A

H

V

I

K

Q

D

N

E

E

K

R

D

D

P

P

H

E

L

L

I

V

A

A

G

H

A

A

G

R

V

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

P

Y

P

-

K

-

E

-

G

-

A

T

S

G

S

D

V

I

E

D

L

S

M

F

K

R

E

D

A

V

T

V

L

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

V

N

D

T

G

D

E

E

I

E

F

F

L

L

K

Q

Q

M

L

I

W

K

E

D

Q

A

I

M

H

E

I

-

G

A

G

G

C

A

A

A

G

G

N

V

A

A

T
x
V

G
|
G

R
|
R

N

N

I

I

H

F

Q

Q

K

H

S

-

L

-

D

D

E

D

A

V

V

V

R

G

M

I

C

T

N

R

A

A

I

V

Y

C

A

K

I

I

T

V

V

H

Q

E

D

N

A

A

S

D

I

V

E

E

A

A

V

L

K

K

I

E

Y

I

E

R

K

K

binding 1,6-di-o-phosphono-d-allitol: Y153 (= Y175), R155 (= R177), K184 (= K206), G209 (≠ A236), G210 (= G237), V236 (≠ T264), G237 (= G265), R238 (= R266)

Sites not aligning to the query:

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

Query Sequence

>WP_109967688.1 NCBI__GCF_003173355.1:WP_109967688.1
MSKSIYVPLDVPKDQQKTYTSNFKTITHESGRLMLFAGDQKIEHLNADFFGDGIHKDDND
PEHLFRIAAKAKIGCFATQLGLIARYGADYPDVPYLVKINSKTNLVGTSQQEPSSGLLNT
VEQVVRFRKSSGLKIGGIGYTIYLGSEAESEMLSAAANAIFEAHQNGLVTVLWIYPRGKA
VKDEKDPHLIAGAAGVAACLGSDFVKVNPPKKEGASSVELMKEATLAAGRTKVVCAGGSS
VDGEIFLKQLWEQIHIGGCAGNATGRNIHQKSLDEAVRMCNAIYAITVQDASIEEAVKIY
EKK

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