SitesBLAST
Comparing Ac3H11_493 FitnessBrowser__acidovorax_3H11:Ac3H11_493 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6b9uA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase from brucella melitensis complexed with nadh
40% identity, 99% coverage: 3:253/253 of query aligns to 2:244/244 of 6b9uA
- active site: G15 (= G16), S142 (= S142), L152 (= L152), Y155 (= Y155), K159 (= K159)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G12), S14 (≠ N15), G15 (= G16), F16 (≠ I17), D35 (= D36), R36 (≠ I37), A57 (= A61), D58 (= D62), I59 (≠ V63), N85 (= N89), A86 (= A90), V140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), A187 (≠ F187), G188 (≠ N188), T190 (= T191), P191 (≠ G192), L192 (= L193), F196 (= F197)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 98% coverage: 3:250/253 of query aligns to 3:244/248 of 6ixmC
- active site: G16 (= G16), S142 (= S142), Y155 (= Y155), K159 (= K159)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (≠ N15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (= I37), A61 (= A61), D62 (= D62), T63 (≠ V63), N89 (= N89), A90 (= A90), M140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), A186 (≠ V186), Y187 (≠ F187), I188 (≠ N188), L192 (≠ G192)
7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
41% identity, 98% coverage: 3:250/253 of query aligns to 3:247/251 of 7djsD
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G16 (= G16), I17 (= I17), D36 (= D36), L37 (≠ I37), C61 (≠ A61), D62 (= D62), V63 (= V63), N89 (= N89), A90 (= A90), T140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), A186 (vs. gap), V187 (= V186)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
37% identity, 99% coverage: 1:250/253 of query aligns to 1:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), Q15 (≠ N15), G16 (= G16), I17 (= I17), D36 (= D36), V63 (= V63), N89 (= N89), A91 (≠ G91), S94 (vs. gap), I142 (= I140), S143 (≠ A141), S144 (= S142), Y157 (= Y155), K161 (= K159), P187 (= P185), H188 (≠ T191), I190 (≠ L193), I194 (≠ F197)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
39% identity, 98% coverage: 2:250/253 of query aligns to 8:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G12), S20 (≠ G14), K21 (≠ N15), G22 (= G16), I23 (= I17), A43 (≠ I37), S44 (≠ N38), S45 (vs. gap), G68 (≠ A61), D69 (= D62), V70 (= V63), N96 (= N89), S97 (≠ A90), G98 (= G91), Y100 (≠ H94), I144 (= I140), S146 (= S142), Y159 (= Y155), K163 (= K159), P189 (= P185), G190 (≠ V186), M191 (≠ F187), I192 (≠ N188), T194 (≠ D190), G196 (= G192), T197 (≠ E196)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S142), Y159 (= Y155), M191 (≠ F187), I202 (≠ P201)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
38% identity, 97% coverage: 6:250/253 of query aligns to 5:243/246 of 3osuA
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 99% coverage: 1:250/253 of query aligns to 1:244/248 of 4urfB
- active site: G16 (= G16), S142 (= S142), I152 (≠ L152), Y155 (= Y155), K159 (= K159)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (= L216), R211 (≠ G217), R212 (= R218)
- binding bicarbonate ion: I92 (≠ W92), G94 (≠ H94), R109 (≠ K109), R179 (= R179), S228 (= S234)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (= G14), N15 (= N15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (= I37), D62 (= D62), T63 (≠ V63), N89 (= N89), A90 (= A90), G91 (= G91), I140 (= I140), Y155 (= Y155), K159 (= K159), P185 (= P185), A186 (≠ V186), I188 (≠ P189), T190 (= T191)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 99% coverage: 1:250/253 of query aligns to 1:244/248 of 4urfA
- active site: G16 (= G16), S142 (= S142), I152 (≠ L152), Y155 (= Y155), K159 (= K159)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ W92), S93 (≠ T93), G94 (≠ H94), E95 (≠ R95), T97 (≠ R97), E101 (= E101), T103 (≠ S103), Q106 (≠ E106), R109 (≠ K109), S175 (≠ P175), G177 (≠ N177)
- binding magnesium ion: S237 (≠ V243), Y238 (≠ C244)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (= G14), N15 (= N15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (= I37), W41 (≠ G41), D62 (= D62), T63 (≠ V63), N89 (= N89), A90 (= A90), G91 (= G91), I140 (= I140), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (≠ P189), T190 (= T191)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 99% coverage: 1:250/253 of query aligns to 1:244/248 of 4ureB
- active site: G16 (= G16), S142 (= S142), I152 (≠ L152), Y155 (= Y155), K159 (= K159)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (= N15), G16 (= G16), I17 (= I17), N89 (= N89), G91 (= G91), Y155 (= Y155), P185 (= P185), A186 (≠ V186)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
34% identity, 100% coverage: 1:253/253 of query aligns to 1:243/244 of 7krmC
- active site: G18 (= G16), S140 (= S142), Y155 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (≠ N15), G18 (= G16), I19 (= I17), D38 (= D36), L39 (≠ I37), A60 (= A61), N61 (≠ D62), V62 (= V63), N88 (= N89), V111 (≠ I113), S140 (= S142), Y155 (= Y155), K159 (= K159), I188 (≠ F187), T190 (≠ P189)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
38% identity, 97% coverage: 6:250/253 of query aligns to 2:236/239 of 3sj7A
- active site: G12 (= G16), S138 (= S142), Q148 (≠ L152), Y151 (= Y155), K155 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (≠ G14), R11 (≠ N15), I13 (= I17), N31 (= N35), Y32 (≠ D36), A33 (≠ I37), G34 (vs. gap), S35 (≠ N38), A58 (= A61), N59 (≠ D62), V60 (= V63), N86 (= N89), A87 (= A90), T109 (≠ I113), S138 (= S142), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (≠ E196)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
33% identity, 98% coverage: 2:250/253 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G16), N111 (= N114), S139 (= S142), Q149 (≠ L152), Y152 (= Y155), K156 (= K159)
- binding acetoacetyl-coenzyme a: D93 (≠ N96), K98 (≠ E101), S139 (= S142), N146 (≠ R149), V147 (≠ P150), Q149 (≠ L152), Y152 (= Y155), F184 (= F187), M189 (≠ L193), K200 (= K209)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (= N15), G18 (= G16), I19 (= I17), D38 (= D36), F39 (≠ I37), V59 (≠ A61), D60 (= D62), V61 (= V63), N87 (= N89), A88 (= A90), G89 (= G91), I90 (≠ W92), T137 (≠ I140), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), F184 (= F187), T185 (≠ N188), T187 (= T191), M189 (≠ L193)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
33% identity, 99% coverage: 1:250/253 of query aligns to 3:251/255 of 5itvA
- active site: G18 (= G16), S141 (= S142), Y154 (= Y155), K158 (= K159)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (≠ N15), G18 (= G16), I19 (= I17), D38 (= D36), I39 (= I37), T61 (≠ A61), I63 (≠ V63), N89 (= N89), G91 (= G91), T139 (≠ I140), S141 (= S142), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (≠ V186), I186 (≠ F187), I187 (≠ P189)
Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
39% identity, 97% coverage: 5:250/253 of query aligns to 2:252/256 of Q48436
- 6:33 (vs. 9:36, 54% identical) binding
- D59 (= D62) binding
- K156 (= K159) binding
1gegE Cryatal structure analysis of meso-2,3-butanediol dehydrogenase (see paper)
39% identity, 97% coverage: 5:250/253 of query aligns to 2:252/256 of 1gegE
- active site: G13 (= G16), S139 (= S142), Y152 (= Y155), K156 (= K159), V197 (≠ A194)
- binding alpha-D-glucopyranose: R63 (≠ S66), D64 (≠ A67), F67 (≠ K70), E123 (≠ P127)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), Q12 (≠ N15), I14 (= I17), D33 (= D36), Y34 (≠ I37), V58 (≠ A61), D59 (= D62), V60 (= V63), N86 (= N89), A87 (= A90), I109 (= I113), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (vs. gap), V185 (≠ C182), T187 (≠ N184), M189 (≠ V186)
H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
35% identity, 99% coverage: 1:250/253 of query aligns to 1:240/251 of H9XP47
- N15 (= N15) binding
- M17 (≠ I17) binding
- D36 (= D36) binding
- D60 (= D62) binding
- V61 (= V63) binding
- N87 (= N89) binding
- S138 (= S142) binding ; binding
- V139 (≠ T143) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A144) binding
- Y151 (= Y155) binding ; binding ; binding
- K155 (= K159) binding
- V184 (vs. gap) binding
- T186 (vs. gap) binding
- RDK 197:199 (≠ RAK 207:209) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
Sites not aligning to the query:
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
35% identity, 100% coverage: 1:253/253 of query aligns to 1:247/247 of 4jroC
- active site: G16 (= G16), S142 (= S142), Q152 (≠ L152), Y155 (= Y155), K159 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ G14), R15 (≠ N15), G16 (= G16), I17 (= I17), N35 (= N35), Y36 (≠ D36), N37 (≠ I37), G38 (≠ N38), S39 (≠ E39), N63 (≠ D62), V64 (= V63), N90 (= N89), A91 (= A90), I93 (≠ W92), I113 (= I113), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (≠ A194), T190 (≠ E196)
F1SWA0 Zerumbone synthase; EC 1.1.1.326 from Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet) (see paper)
35% identity, 99% coverage: 1:250/253 of query aligns to 1:255/267 of F1SWA0
- S142 (= S142) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- S144 (≠ A144) mutation to A: Increased oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- Y155 (= Y155) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- K159 (= K159) mutation to A: Abolishes all oxidoreductase activity.
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 98% coverage: 2:250/253 of query aligns to 4:242/252 of 6vspB
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 98% coverage: 2:250/253 of query aligns to 2:240/251 of 6vspA
- active site: G16 (= G16), S138 (= S142), Y151 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (= N15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ I37), W37 (≠ I37), A38 (≠ N38), I59 (≠ A61), D60 (= D62), V61 (= V63), N87 (= N89), A88 (= A90), G89 (= G91), V90 (≠ T93), V110 (≠ I113), T136 (≠ I140), S138 (= S142), Y151 (= Y155), K155 (= K159), P181 (= P185), S182 (≠ V186), L183 (≠ F187), V184 (vs. gap), T186 (vs. gap), N187 (= N188), M188 (≠ P189), T189 (≠ D190)
Query Sequence
>Ac3H11_493 FitnessBrowser__acidovorax_3H11:Ac3H11_493
MRVSNKSIIVTGAGNGIGEGIAKRLAAEGGKVIVNDINEAGGQRVVAEITAAGGTAAFFK
ADVTNSAQVKAMVDEAVRLYGRLDVVVNNAGWTHRNRPMLEVSEEEFDKVYAINMKSIYL
SAIHAVPALRQAGGGSIINIASTAGLRPRPGLTWYNGSKGAVIITSKSMAAELGPDNIRV
NCINPVFNPDTGLAAEFAGGPVDDARRAKFLATIPLGRFSTALDVANAALYLASEEASFI
SGVCIEVDGGRCV
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