SitesBLAST

5gmuB Crystal structure of chorismate mutase like domain of bifunctional dahp synthase of bacillus subtilis in complex with chlorogenic acid (see paper)
28% identity, 80% coverage: 6:83/98 of query aligns to 8:85/87 of 5gmuB

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5gmuB

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binding (1R,3R,4S,5R)-3-[3-[3,4-bis(oxidanyl)phenyl]propanoyloxy]-1,4,5-tris(oxidanyl)cyclohexane-1-carboxylic acid: R26 (= R24), R44 (≠ V42), F45 (≠ Y43), D46 (= D44), E50 (= E48), F78 (≠ I76), K79 (≠ D77), L82 (≠ R80), Q85 (≠ E83)

3nvtA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e (see paper)
33% identity, 81% coverage: 5:83/98 of query aligns to 1:74/345 of 3nvtA

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3nvtA

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Sites not aligning to the query:

binding manganese (ii) ion: 114, 284, 310, 321

P39912 Protein AroA(G); EC 2.5.1.54; EC 5.4.99.5 from Bacillus subtilis (strain 168) (see paper)
28% identity, 80% coverage: 6:83/98 of query aligns to 9:86/358 of P39912

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P39912

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Sites not aligning to the query:

2 modified: Phosphoserine

6al9B Crystal structure of chorismate mutase from helicobacter pylori in complex with prephenate
35% identity, 83% coverage: 3:83/98 of query aligns to 5:83/91 of 6al9B

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6al9B

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binding pyruvic acid: I33 (= I31), Q83 (≠ E83)

6al9A Crystal structure of chorismate mutase from helicobacter pylori in complex with prephenate
35% identity, 83% coverage: 3:83/98 of query aligns to 4:82/90 of 6al9A

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binding prephenic acid: R25 (= R24), C43 (≠ D44), R46 (= R47), E47 (= E48), F75 (≠ I76), S78 (= S79), Q82 (≠ E83)

3tfcA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e in complex with phosphoenolpyruvate (see paper)
32% identity, 80% coverage: 6:83/98 of query aligns to 1:73/343 of 3tfcA

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3tfcA

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Sites not aligning to the query:

binding manganese (ii) ion: 113, 283, 309, 320
binding phosphoenolpyruvate: 137, 193, 196, 218, 248, 283

P0A9J8 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 from Escherichia coli (strain K12)
37% identity, 76% coverage: 6:79/98 of query aligns to 10:84/386 of P0A9J8

query
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P0A9J8

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R11 (= R7) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R24) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K35) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E48) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.

Sites not aligning to the query:

88 mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

Query Sequence

>WP_004511889.1 NCBI__GCF_000012925.1:WP_004511889.1
MTIDELRQEIDRMDSELLRIFNRRASLALEIGLIKKERGLPVYDPKREKLIFERMKADNP
GPLDDGAIVRLFERVIDESRRLERIMTHPEETTGKEES

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