SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_089299593.1 NCBI__GCF_900188115.1:WP_089299593.1 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 8 hits to proteins with known functional sites (download)

Q79FW5 PE-PGRS family protein PE_PGRS11; PE-PGRS phosphoglycerate mutase; EC 5.4.2.12 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
30% identity, 97% coverage: 1:203/209 of query aligns to 283:496/584 of Q79FW5

query
sites
Q79FW5

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R289 (= R7) mutation to A: Lack of phosphoglycerate mutase activity.
H290 (= H8) mutation to A: Lack of phosphoglycerate mutase activity.

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
34% identity, 78% coverage: 1:164/209 of query aligns to 2:166/207 of 4ij6A

query
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4ij6A

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active site: R8 (= R7), A9 (≠ H8), N15 (= N14), R58 (= R58), E82 (= E82), H150 (= H154)
binding phosphoserine: R8 (= R7), Q21 (≠ N20), R58 (= R58), E82 (= E82), H85 (≠ V85), H150 (= H154), T151 (≠ G155)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
28% identity, 79% coverage: 3:168/209 of query aligns to 4:164/207 of 1h2fA

query
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1h2fA

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active site: R8 (= R7), H9 (= H8), N15 (= N14), R58 (= R58), E82 (= E82), H150 (= H154)
binding phosphate ion: G142 (≠ E142), E143 (= E143)
binding trivanadate: R8 (= R7), H9 (= H8), N15 (= N14), Q21 (≠ P24), R58 (= R58), E82 (= E82), H150 (= H154), G151 (= G155), V152 (≠ G156)

Sites not aligning to the query:

binding phosphate ion: 1, 2, 3

1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
28% identity, 79% coverage: 3:168/209 of query aligns to 4:164/207 of 1h2eA

query
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1h2eA

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active site: R8 (= R7), H9 (= H8), N15 (= N14), R58 (= R58), E82 (= E82), H150 (= H154)
binding phosphate ion: R8 (= R7), H9 (= H8), R58 (= R58), E82 (= E82), H150 (= H154)

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
27% identity, 96% coverage: 2:201/209 of query aligns to 3:207/209 of 4qihA

query
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4qihA

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active site: H9 (= H8), R58 (= R58), E82 (= E82)
binding vanadate ion: R8 (= R7), H9 (= H8), Q21 (≠ N20), R58 (= R58), H157 (= H154)

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
29% identity, 74% coverage: 2:156/209 of query aligns to 4:160/217 of 4pzaB

query
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4pzaB

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active site: H10 (= H8), R59 (= R58), E83 (= E82)
binding phosphate ion: R9 (= R7), H10 (= H8), R59 (= R58), E83 (= E82), H158 (= H154), G159 (= G155)

P9WIC7 Glucosyl-3-phosphoglycerate phosphatase; Mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; EC 3.1.3.70 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 74% coverage: 2:156/209 of query aligns to 5:161/223 of P9WIC7

query
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P9WIC7

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L

D

V

L

V

Q

R

V

V

I

D

D

T

G

R

V

L

H

R

E

E

V

T

F

H

V

L

G

G

Q

D

L

W

E

Q

D

G

R

L

T

T

D

H

R

A

E

Q

G

I

V

D

E

A

A

D

Y

A

A

P

Q

G

V

A

F

R

L

L

P

A

W

W

I

R

Q

E

G

-

E

D

L

A

H

T

H

W

T

A

M

P

P

H

G

G

E

E

S

S

G

R

I

V

E

D

V

V

R

A

D

A

R

R

F

S

V

R

A

P

A

L

I

V

S

A

E

E

V

L

R

V

A

A

K

S

H

E

E

P

E

E

-

W

-

G

-

A

E

D

D

E

P

P

D

D

G

R

T

P

V

V

M

L

V

V

S

A

H
|
H

G

G

R10 (= R7) mutation to A: Loss of phosphatase activity.
H11 (= H8) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N14) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ R44) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R58) mutation to A: Loss of phosphatase activity.
H159 (= H154) mutation to A: About 5% of wild-type phosphatase activity.

Sites not aligning to the query:

209 L→E: Disrupts dimerization of the enzyme, which exists as a monomer and has lost its ability to perform dephosphorylation.

Q9HIJ2 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) (see paper)
30% identity, 44% coverage: 5:95/209 of query aligns to 6:96/200 of Q9HIJ2

query
sites
Q9HIJ2

L

L

V

I

R

R

H
|
H

A

G

E

E

S

S

T

D

A

I

N

N

V

V

R

K

K

G

A

I

I

L

N

S

T

D

R

T

L

I

P

D

G

N

P

N

P

M

L

L

S

T

D

E

V

K

G

G

R

M

Q

R

Q

Q

A

A

D

E

E

H

L

A

A

A

R

E

L

L

R

K

S

G

E

I

P

D

V

I

V

K

A

N

V

F

Y

Y

S

S

L

P

A

I

T

K

R

R

A

A

Q

F

Q

D

T

T

A

A

T

Q

P

I

V

I

A

A

A

D

A

S

H

F

G

N

V

K

D

D

L

V

Q

V

V

T

I

D

D

Q

G

R

V

L

H

I

E

E

V

I

F

G

V

L

G

G

Q

K

L

A

E

R

D

G

R

R

T

K

D

A

R

N

E

E

H9 (= H8) mutation to A: Loss of activity.

Query Sequence

>WP_089299593.1 NCBI__GCF_900188115.1:WP_089299593.1
MKLKLVRHAESTANVRKAINTRLPGPPLSDVGRQQADELAARLRSEPVVAVYSSLATRAQ
QTATPVAAAHGVDLQVIDGVHEVFVGQLEDRTDREGVEAYAQVFLPWIQGELHHTMPGGE
SGIEVRDRFVAAISEVRAKHEEEDPDGTVVMVSHGGVMRLGVELLADNVPRSGRVSGLIA
NTGAVVLEAHRDGRWRCVAWDGVDLSGHG

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