SitesBLAST

G3XD01 UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase; UDP-D-GlcNAc3NA N-acetyltransferase; UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronic acid 3-N-acetyltransferase; EC 2.3.1.201 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
31% identity, 43% coverage: 58:168/258 of query aligns to 25:152/191 of G3XD01

query
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G3XD01

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K136 (= K152) mutation to A: Reduction in catalytic activity.; mutation to R: No effect on catalytic activity.

4mzuF Crystal structure of fdtd, a bifunctional ketoisomerase/n- acetyltransferase from shewanella denitrificans (see paper)
35% identity, 32% coverage: 85:167/258 of query aligns to 58:140/294 of 4mzuF

query
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4mzuF

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binding coenzyme a: N81 (≠ G108), D82 (≠ T109), K83 (≠ S110), G100 (= G127), A101 (= A128), L106 (= L133), G118 (= G145), A119 (≠ S146), T124 (= T151), K125 (= K152), I134 (≠ V161), N136 (≠ I163), R139 (= R166)

Sites not aligning to the query:

binding thymine: 20, 21, 38
binding thymidine-5'-diphosphate: 189, 203, 205, 270

4mzuB Crystal structure of fdtd, a bifunctional ketoisomerase/n- acetyltransferase from shewanella denitrificans (see paper)
30% identity, 36% coverage: 86:178/258 of query aligns to 47:152/290 of 4mzuB

query
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4mzuB

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binding coenzyme a: F72 (vs. gap), T80 (≠ N112), N81 (≠ K113), D82 (≠ G114), K83 (= K115), P85 (≠ H117), G99 (= G127), A100 (= A128), G117 (= G145), A118 (≠ S146), T123 (= T151), K124 (= K152), I133 (≠ V161), R138 (= R166)
binding magnesium ion: G58 (≠ D97), N76 (≠ G108)

Sites not aligning to the query:

binding coenzyme a: 199
binding thymine: 20, 21, 38, 39
binding thymidine-5'-diphosphate: 171, 176, 189, 191, 202, 203, 270

3mqhA Crystal structure of the 3-n-acetyl transferase wlbb from bordetella petrii in complex with coa and udp-3-amino-2-acetamido-2,3-dideoxy glucuronic acid (see paper)
31% identity, 40% coverage: 65:168/258 of query aligns to 32:152/191 of 3mqhA

query
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3mqhA

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binding coenzyme a: F76 (vs. gap), T84 (vs. gap), N85 (vs. gap), V86 (vs. gap), Y87 (vs. gap), P89 (vs. gap), G111 (= G127), A112 (= A128), A130 (≠ S146), N135 (≠ T151), V145 (= V161), P148 (= P164), R150 (= R166)
binding (2S,3S,4R,5R,6R)-5-(acetylamino)-4-amino-6-{[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-3-hydroxytetrahydro-2H-pyran-2-carboxylic acid: F46 (= F79), Q60 (≠ G95), N61 (= N96), Y66 (= Y101), F76 (vs. gap), N85 (vs. gap), V86 (vs. gap), R95 (≠ W111), Y99 (≠ K115)

Sites not aligning to the query:

Query Sequence

>AO353_15825 FitnessBrowser__pseudo3_N2E3:AO353_15825
MFERLREDIQSVFHRDPAARNAFEVLTCYPGMHAIWIHRLSAALWGMGWKWLARLVSNFG
RWLTGIEIHPGAKVGRRFFIDHGMGIVIGETAEIGNDVTLYQGVTLGGTSWNKGKRHPTL
EDGVVVGAGAKVLGPFTVGAGAKVGSNAVVTKAVPAGATVVGIPGRIIVKSDDELEARRK
AMAEKIGFDAYGVSEDMPDPVARAIGQLLDHLQAVDGRLEGMCGALKDLGSPYCAKDLPE
LREEDFACVKGKDESQAS

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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