SitesBLAST

P07464 Galactoside O-acetyltransferase; GAT; Acetyl-CoA:galactoside 6-O-acetyltransferase; Thiogalactoside acetyltransferase; Thiogalactoside transacetylase; EC 2.3.1.18 from Escherichia coli (strain K12) (see 3 papers)
34% identity, 57% coverage: 70:165/168 of query aligns to 85:182/203 of P07464

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P07464

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N85 (≠ G70) binding in other chain; binding in other chain
D93 (≠ P78) binding
H115 (≠ V99) mutation to A: Results in an 1800-fold decrease in catalytic activity.
S142 (≠ A125) binding in other chain
A160 (= A143) binding in other chain
TK 165:166 (= TK 148:149) binding
R180 (= R163) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed; Partial
17 binding
71 binding
183 binding in other chain

1krrA Galactoside acetyltransferase in complex with acetyl-coenzyme a (see paper)
34% identity, 57% coverage: 70:165/168 of query aligns to 84:181/200 of 1krrA

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1krrA

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binding acetyl coenzyme *a: N84 (≠ G70), I103 (= I89), A104 (≠ G90), P105 (≠ Q91), T112 (≠ Q97), H114 (≠ V99), G140 (= G124), S141 (≠ A125), N146 (≠ I130), G158 (= G142), A159 (= A143), A174 (≠ V158), P177 (= P161)

Sites not aligning to the query:

binding acetyl coenzyme *a: 182

1krvA Galactoside acetyltransferase in complex with coa and pnp-beta-gal (see paper)
34% identity, 57% coverage: 70:165/168 of query aligns to 84:181/201 of 1krvA

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binding 4-nitrophenyl beta-D-galactopyranoside: N84 (≠ G70), V90 (≠ Y76), D92 (≠ P78), M126 (≠ E111)
binding coenzyme a: A104 (≠ G90), S110 (≠ R96), T112 (≠ Q97), W138 (≠ E122), G140 (= G124), S141 (≠ A125), N146 (≠ I130), A159 (= A143), P177 (= P161), R179 (= R163)

Sites not aligning to the query:

1kruA Galactoside acetyltransferase in complex with iptg and coenzyme a (see paper)
34% identity, 57% coverage: 70:165/168 of query aligns to 84:181/201 of 1kruA

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binding coenzyme a: H114 (≠ V99), W138 (≠ E122), G140 (= G124), S141 (≠ A125), G158 (= G142), A159 (= A143), P177 (= P161)
binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N84 (≠ G70), V90 (≠ Y76), D92 (≠ P78), L102 (≠ I88), H114 (≠ V99), M126 (≠ E111)

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4hzdA Crystal structure of serine acetyltransferase in complex with coenzyme a from brucella abortus strain s19 (see paper)
30% identity, 66% coverage: 55:165/168 of query aligns to 136:244/250 of 4hzdA

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binding coenzyme a: H158 (= H77), G203 (= G124), A204 (= A125), A221 (≠ G142), A222 (= A143), T235 (≠ I156), A237 (≠ V158), I244 (≠ L165)
binding magnesium ion: S224 (≠ T145), A237 (≠ V158), G238 (= G159)

4h7oA Crystal structure of serine acetyltransferase from vibrio cholerae o1 biovar el tor n16961
27% identity, 90% coverage: 15:165/168 of query aligns to 82:240/258 of 4h7oA

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binding arginine: Y127 (≠ V48), Q131 (≠ I52)
binding cysteine: D88 (≠ K21), P89 (≠ I22), D153 (≠ Y76), H154 (= H77), G180 (≠ S103), R188 (≠ A113), H189 (≠ S114)

Sites not aligning to the query:

binding arginine: 51, 53

4aawA S.Pneumoniae glmu in complex with an antibacterial inhibitor (see paper)
41% identity, 49% coverage: 87:168/168 of query aligns to 360:442/455 of 4aawA

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4aawA

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binding 4-{[1-(2-{[({5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl}sulfonyl)amino]methyl}phenyl)piperidin-4-yl]methoxy}-4-oxobutanoic acid: V380 (vs. gap), Y382 (≠ S107), D383 (≠ Q108), I405 (= I130)

Sites not aligning to the query:

active site: 14

7kr9A Bifunctional enzyme glmu bound to zn(ii) (see paper)
41% identity, 49% coverage: 87:168/168 of query aligns to 358:440/453 of 7kr9A

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7kr9A

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binding acetyl coenzyme *a: Y359 (≠ I88), V378 (vs. gap), N379 (≠ D106), Y380 (≠ S107)

Sites not aligning to the query:

binding zinc ion: 309, 324

Query Sequence

>BWI76_RS05560 FitnessBrowser__Koxy:BWI76_RS05560
MFEAIRQVGQEIKSCGGIKAKIAVLLYRLATLYRSRNPLWKICGIPFVILNIVINECLFC
IELPWRARIGYGLKLYHPHCIVINRGTIIGQNCTLRQGVTIGSVTDSQGRESASPRIGDN
VEFGAHAVVIGAVTLGDNVKVGAGTVVTKDLAAGMIAVGQPYRVLNGD

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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