SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012407009.1 NCBI__GCF_000020025.1:WP_012407009.1 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)

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)
64% identity, 98% coverage: 9:360/360 of query aligns to 2:350/350 of P0A991

query
sites
P0A991

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K208 (= K214) modified: N6-acetyllysine
K237 (= K242) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to A: Loss of activity.
K239 (= K244) mutation to A: No change in activity.
K262 (≠ E273) modified: N6-acetyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

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, 54% coverage: 68:261/360 of query aligns to 12:196/263 of P58315

query
sites
P58315

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W144 (= W205) mutation to E: Loss of FBP aldolase activity; when associated with F-146.
Y146 (= Y207) 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, 54% coverage: 68:261/360 of query aligns to 10:194/255 of 2yceE

query
sites
2yceE

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binding d-mannitol-1,6-diphosphate: D22 (= D80), H23 (≠ Q81), H27 (= H85), W142 (= W205), R146 (= R209), K175 (= K242), K177 (= K244)

Sites not aligning to the query:

binding d-mannitol-1,6-diphosphate: 201, 202, 228, 229, 230

1w8sA The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates (see paper)
30% identity, 54% coverage: 68:261/360 of query aligns to 10:194/250 of 1w8sA

query
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1w8sA

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binding 1,6-di-O-phosphono-beta-D-fructofuranose: A20 (≠ P78), D22 (= D80), H23 (≠ Q81), H27 (= H85), R146 (= R209), K175 (= K242), K177 (= K244)

Sites not aligning to the query:

binding 1,6-di-O-phosphono-beta-D-fructofuranose: 200, 201, 202, 228, 229, 230

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)
26% identity, 74% coverage: 72:336/360 of query aligns to 21:251/281 of P58314

query
sites
P58314

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G

G

L

A

I

V

S

V

G

G

R

R

K

N

T

I

F

F

Q

Q

R

R

K191 (= K265) mutation to A: Loss of activity.

2qjgA M. Jannaschii adh synthase complexed with f1,6p (see paper)
25% identity, 82% coverage: 56:351/360 of query aligns to 7:263/272 of 2qjgA

query
sites
2qjgA

L

I

R

K

N

N

L

L

Q

G

L

K

L

L

Y

V

S

R

T

L

G

E

R

R

L

I

A

F

N

N

-

R

-

E

T

S

G

E

Y

K

L

T

S

V

I

I

L

V

P

P

V

M

D

D

Q
x
H

G

G

I

V

E

-

H

-

S

-

A

-

G

-

A

-

S
|
S

F

N

A

G

P

P

N

I

P

K

I

G

Y

L

F

I

D

D

P

I

E

R

N

K

I

T

V

V

R

N

L

D

A

V

I

A

A

E

A

G

G

G

C

A

N

N

A

A

V

V

A

L

T

L

T

H

L

K

G

G

V

I

L

V

G

R

I

H

V

G

S

H

R

R

K

G

Y

Y

A

G

H

K

K

D

I

V

P

G

F

L

I

I

A

I

K

H

I

L

N

S

H

G

N

G

E

T

L

A

L

I

T

S

F

-

P

P

N

N

Q

P

F

L

D

K

Q

K

V

V

L

I

F

V

A

T

D

T

V

V

E

E

Q

E

A

A

W

I

N

R

L

M

G

G

A

A

A

D

A

A

V

V

G

S

A

I

T

H

I

V

Y

N

F

V

G

G

S

S

D

D

Q

E

S

D

T

W

R

E

Q

A

I

Y

Q

R

E

D

I

L

S

G

K

M

A

I

F

A

K

E

R

T

A

C

H

E

E

Y

L

W

G

G

M

M

A

P

T

L

I

I

L

A

W

M

C

M

Y
|
Y

L

P

R
|
R

N

G

N

K

A

H

F

I

K

Q

Q

N

D

E

K

R

D

D

Y

P

H

E

L

L

A

V

A

A

D

-

L

-

T

-

G

-

Q

H

A

A

N

A

H

R

L

L

G

G

V

A

T

E

I

L

E

G

A

A

D

D

I

I

I

V

K
|
K

Q

-

K

-

L

-

P

-

E

-

N

-

G

-

Y

-

G

-

A

-

V

-

A

-

K

-

A

-

S

-

G

-

K

-

S

-

Y

-

G

-

K

-

T

-

D

-

E

-

R

-

V

-

Y

-

T

T

E

S

L

Y

T

T

T

G

D

D

H

-

P

-

I

I

D

D

L

S

T

F

R

R

Y

D

Q

V

V

V

L

K

N

G

C

C

Y

P

S

A

G

-

R

-

V

-

G

P

L

V

I

V

N

V

S

A

G
|
G

A

P

T

K

G

T

K

N

N

T

D

D

-

E

F

F

A

L

E

Q

A

M

I

I

R

K

T

D

A

A

V

M

I

-

N

-

K

-

R

E

A

A

G

G

G

A

S

A

G

G

L

V

I

A

S
x
V

G
|
G

R
|
R

K

N

T

I

F

F

Q

Q

R

H

P

D

F

D

E

V

G

G

V

I

-

T

-

R

-

A

-

V

-

C

K

K

L

I

F

V

H

H

T

E

I

N

Q

A

D

D

V

V

binding 1,6-di-o-phosphono-d-allitol: H34 (≠ Q81), S37 (= S90), Y153 (= Y207), R155 (= R209), K184 (= K242), G209 (= G301), G210 (= G302), V236 (≠ S329), G237 (= G330), R238 (= R331)

Query Sequence

>WP_012407009.1 NCBI__GCF_000020025.1:WP_012407009.1
MTTTLIESSSIESLLGKEAEDLLTYKAKVSQNLLHLPGPDFVDRIWINSDRNPQVLRNLQ
LLYSTGRLANTGYLSILPVDQGIEHSAGASFAPNPIYFDPENIVRLAIAAGCNAVATTLG
VLGIVSRKYAHKIPFIAKINHNELLTFPNQFDQVLFADVEQAWNLGAAAVGATIYFGSDQ
STRQIQEISKAFKRAHELGMATILWCYLRNNAFKQDKDYHLAADLTGQANHLGVTIEADI
IKQKLPENNNGYGAVAKASGKSYGKTDERVYTELTTDHPIDLTRYQVLNCYSGRVGLINS
GGATGKNDFAEAIRTAVINKRAGGSGLISGRKTFQRPFEEGVKLFHTIQDVYLSPDVTIA

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