SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_007474421.1 NCBI__GCF_000170735.1:WP_007474421.1 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 9 hits to proteins with known functional sites (download)

5ygeA Arga complexed with acecoa and glutamate (see paper)
45% identity, 46% coverage: 59:131/158 of query aligns to 58:130/169 of 5ygeA

query
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5ygeA

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binding acetyl coenzyme *a: I73 (= I74), V76 (≠ L77), A77 (= A78), V78 (= V79), T83 (≠ Q84), G84 (≠ L85), H85 (≠ K86), G86 (= G87), G88 (= G89), H89 (≠ K90), T111 (= T112), E113 (≠ K114), F117 (= F118)
binding glutamic acid: H64 (= H65), R74 (= R75)

Sites not aligning to the query:

6addA The crystal structure of rv2747 from mycobacterium tuberculosis in complex with coa and nlq (see paper)
45% identity, 46% coverage: 59:131/158 of query aligns to 57:129/168 of 6addA

query
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6addA

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binding coenzyme a: V75 (≠ L77), A76 (= A78), V77 (= V79), T82 (≠ Q84), G83 (≠ L85), H84 (≠ K86), G85 (= G87), G87 (= G89), H88 (≠ K90), T110 (= T112), E112 (≠ K114), F115 (= F117)
binding n~2~-acetyl-l-glutamine: T74 (≠ S76), L109 (= L111)

Sites not aligning to the query:

binding coenzyme a: 1, 24, 28
binding n~2~-acetyl-l-glutamine: 27, 28, 30, 147

5yo2A The crystal structure of rv2747 from mycobacterium tuberculosis in complex with acetyl coa and l-arginine (see paper)
45% identity, 46% coverage: 59:131/158 of query aligns to 57:129/168 of 5yo2A

query
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5yo2A

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binding acetyl coenzyme *a: I72 (= I74), R73 (= R75), T74 (≠ S76), V75 (≠ L77), V77 (= V79), T82 (≠ Q84), G83 (≠ L85), H84 (≠ K86), G85 (= G87), G87 (= G89), H88 (≠ K90), T110 (= T112), E112 (≠ K114), F115 (= F117), F116 (= F118)
binding arginine: R73 (= R75), L109 (= L111)

Sites not aligning to the query:

binding acetyl coenzyme *a: 24, 28
binding arginine: 26, 29, 30, 147

P0A6C5 Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli (strain K12) (see paper)
26% identity, 80% coverage: 9:135/158 of query aligns to 297:425/443 of P0A6C5

query
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P0A6C5

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Sites not aligning to the query:

15 H→Y: In EE17.
19 Y→C: In EE51.
54 S→N: In PT2M217.
58 R→H: In EE11.
287 G→S: In PT2M216.
432 Q→R: In PT2M217.

4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
26% identity, 75% coverage: 17:135/158 of query aligns to 284:404/424 of 4i49A

query
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binding (2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14,20-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaicosan-20-yl}amino)pentanedioic acid (non-preferred name): I300 (= I33), L301 (≠ I34), L302 (= L35), R304 (= R37), A343 (≠ R75), C344 (≠ S76), L345 (= L77), A346 (= A78), V347 (= V79), Q352 (= Q84), D353 (≠ L85), G355 (= G87), G357 (= G89), E358 (≠ K90), L379 (= L111), S380 (vs. gap), T383 (≠ K114), W386 (≠ F117), F387 (= F118)

Sites not aligning to the query:

binding (2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14,20-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaicosan-20-yl}amino)pentanedioic acid (non-preferred name): 413, 415

3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
26% identity, 75% coverage: 17:135/158 of query aligns to 284:404/424 of 3d2mA

query
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3d2mA

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binding coenzyme a: L345 (= L77), V347 (= V79), Q352 (= Q84), D353 (≠ L85), G355 (= G87), G357 (= G89), E358 (≠ K90), S380 (vs. gap), T383 (≠ K114), W386 (≠ F117)
binding glutamic acid: L302 (= L35), R304 (= R37), A343 (≠ R75), C344 (≠ S76), L379 (= L111)

Sites not aligning to the query:

active site: 26
binding glutamic acid: 413, 415

3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
26% identity, 75% coverage: 17:135/158 of query aligns to 284:404/424 of 3b8gA

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3b8gA

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binding coenzyme a: I300 (= I33), L345 (= L77), V347 (= V79), Q352 (= Q84), D353 (≠ L85), G355 (= G87), Y356 (≠ I88), G357 (= G89), E358 (≠ K90), S380 (vs. gap), T383 (≠ K114), E385 (= E116), W386 (≠ F117)
binding n-acetyl-l-glutamate: L302 (= L35), R304 (= R37), A343 (≠ R75), C344 (≠ S76), L379 (= L111)

Sites not aligning to the query:

active site: 26
binding n-acetyl-l-glutamate: 413, 415

2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
26% identity, 75% coverage: 17:135/158 of query aligns to 284:404/424 of 2r8vA

query
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binding acetyl coenzyme *a: I300 (= I33), L301 (≠ I34), L345 (= L77), V347 (= V79), Q352 (= Q84), D353 (≠ L85), G355 (= G87), G357 (= G89), E358 (≠ K90), T383 (≠ K114), E385 (= E116), W386 (≠ F117), F387 (= F118)

Sites not aligning to the query:

active site: 26

3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
26% identity, 75% coverage: 17:135/158 of query aligns to 292:408/424 of 3d2pA

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3d2pA

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K

G

E
|
E

F
x
W

F

F

E

A

K

E

L

R

G

G

F

F

V

Q

E

T

I

A

Q

S

K

E

E

D

A

E

V

L

P

P

D

E

K

T

K

R

binding coenzyme a: L303 (≠ Y28), L349 (= L77), V351 (= V79), Q356 (= Q84), D357 (≠ L85), G359 (= G87), G361 (= G89), E362 (≠ K90), E389 (= E116), W390 (≠ F117)

Sites not aligning to the query:

active site: 26
binding arginine: 13, 197, 216, 253, 266, 267, 269, 270, 271, 274, 276

Query Sequence

>WP_007474421.1 NCBI__GCF_000170735.1:WP_007474421.1
MRFYGEIMKIIKPTLREIIDIKTVLKPYVDEGIILNRSDDEIATNIRSYQIVYDKKRPIG
VGALHIYSPYLGEIRSLAVNKEYQLKGIGKELVRNLLKEAKELGLKEVLVLTYKKEFFEK
LGFVEIQKEAVPDKKIWADCIKCKFFPSCNEIALITYL

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