SitesBLAST
Comparing BPHYT_RS05365 FitnessBrowser__BFirm:BPHYT_RS05365 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
47% identity, 99% coverage: 3:252/252 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 (= S15), G15 (= G16), F16 (= F17), D35 (= D36), R36 (≠ L37), A57 (≠ G61), D58 (≠ N62), I59 (≠ V63), N85 (= N89), A86 (= A90), V140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), A187 (≠ I187), G188 (= G188), T190 (= T190), P191 (≠ A191), L192 (= L192), F196 (= F196)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
40% identity, 98% coverage: 2:249/252 of query aligns to 8:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G12), S20 (≠ G14), K21 (≠ S15), G22 (= G16), I23 (≠ F17), A43 (≠ L37), S44 (≠ N38), S45 (≠ G39), G68 (= G61), D69 (≠ N62), V70 (= V63), N96 (= N89), S97 (≠ A90), G98 (= G91), Y100 (≠ H94), I144 (= I140), S146 (= S142), Y159 (= Y155), K163 (= K159), P189 (= P185), G190 (vs. gap), M191 (vs. gap), I192 (≠ V186), T194 (≠ G188), G196 (≠ T190), T197 (≠ A191)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S142), Y159 (= Y155), M191 (vs. gap), I202 (≠ F196)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
38% identity, 99% coverage: 1:249/252 of query aligns to 1:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), Q15 (≠ S15), G16 (= G16), I17 (≠ F17), D36 (= D36), V63 (= V63), N89 (= N89), A91 (≠ G91), S94 (≠ T92), I142 (= I140), S143 (≠ A141), S144 (= S142), Y157 (= Y155), K161 (= K159), P187 (= P185), H188 (≠ T190), I190 (≠ L192), I194 (≠ F196)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
40% identity, 100% coverage: 1:252/252 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 (≠ S15), G16 (= G16), I17 (≠ F17), N35 (= N35), Y36 (≠ D36), N37 (≠ L37), G38 (≠ N38), S39 (≠ G39), N63 (= N62), V64 (= V63), N90 (= N89), A91 (= A90), I93 (≠ T92), I113 (≠ V113), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (≠ L193), T190 (≠ E195)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
34% identity, 100% coverage: 1:252/252 of query aligns to 1:243/244 of 7krmC
- active site: G18 (= G16), S140 (= S142), Y155 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (= S15), G18 (= G16), I19 (≠ F17), D38 (= D36), L39 (= L37), A60 (≠ G61), N61 (= N62), V62 (= V63), N88 (= N89), V111 (= V113), S140 (= S142), Y155 (= Y155), K159 (= K159), I188 (≠ G188), T190 (= T190)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 98% coverage: 2:249/252 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 (≠ D101), S139 (= S142), N146 (≠ R149), V147 (≠ P150), Q149 (≠ L152), Y152 (= Y155), F184 (≠ I187), M189 (≠ L192), K200 (≠ R208)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ F17), D38 (= D36), F39 (≠ L37), V59 (≠ G61), D60 (≠ N62), V61 (= V63), N87 (= N89), A88 (= A90), G89 (= G91), I90 (≠ T92), T137 (≠ I140), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), F184 (≠ I187), T185 (≠ G188), T187 (= T190), M189 (≠ L192)
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
37% identity, 99% coverage: 1:249/252 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 (= L215), R211 (≠ G216), R212 (= R217)
- binding bicarbonate ion: I92 (≠ T92), G94 (≠ H94), R109 (= R109), R179 (= R179), S228 (= S233)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (= G14), N15 (≠ S15), G16 (= G16), I17 (≠ F17), D36 (= D36), I37 (≠ L37), D62 (≠ N62), T63 (≠ V63), N89 (= N89), A90 (= A90), G91 (= G91), I140 (= I140), Y155 (= Y155), K159 (= K159), P185 (= P185), A186 (≠ V186), I188 (≠ G188), T190 (= T190)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
37% identity, 99% coverage: 1:249/252 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 (≠ T92), S93 (≠ T93), G94 (≠ H94), E95 (≠ R95), T97 (≠ K97), E101 (≠ D101), T103 (= T103), Q106 (≠ E106), R109 (= R109), S175 (≠ P175), G177 (≠ R177)
- binding magnesium ion: S237 (≠ V242), Y238 (≠ C243)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (= G14), N15 (≠ S15), G16 (= G16), I17 (≠ F17), D36 (= D36), I37 (≠ L37), W41 (≠ A41), D62 (≠ N62), T63 (≠ V63), N89 (= N89), A90 (= A90), G91 (= G91), I140 (= I140), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (≠ G188), T190 (= T190)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
37% identity, 99% coverage: 1:249/252 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 (≠ S15), G16 (= G16), I17 (≠ F17), N89 (= N89), G91 (= G91), Y155 (= Y155), P185 (= P185), A186 (≠ V186)
1ahhA 7 alpha-hydroxysteroid dehydrogenase complexed with NAD+ (see paper)
39% identity, 99% coverage: 1:249/252 of query aligns to 7:249/253 of 1ahhA
- active site: G22 (= G16), S146 (= S142), M156 (≠ L152), Y159 (= Y155), K163 (= K159)
- binding nicotinamide-adenine-dinucleotide: G18 (= G12), A21 (≠ S15), D42 (= D36), I43 (≠ L37), C67 (≠ G61), D68 (≠ N62), I69 (≠ V63), N95 (= N89), G97 (= G91), T145 (≠ A141), Y159 (= Y155), K163 (= K159), P189 (= P185), G190 (≠ T190), I192 (≠ L192)
1ahiA 7 alpha-hydroxysteroid dehydrogenase complexed with nadh and 7-oxo glycochenodeoxycholic acid (see paper)
39% identity, 99% coverage: 1:249/252 of query aligns to 7:249/255 of 1ahiA
- active site: G22 (= G16), S146 (= S142), M156 (≠ L152), Y159 (= Y155), K163 (= K159)
- binding glycochenodeoxycholic acid: S146 (= S142), A148 (= A144), N151 (≠ R147), Y159 (= Y155), A196 (≠ F196), V200 (≠ E200)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G18 (= G12), A21 (≠ S15), G22 (= G16), I23 (≠ F17), D42 (= D36), I43 (≠ L37), D68 (≠ N62), I69 (≠ V63), N95 (= N89), Y159 (= Y155), K163 (= K159), P189 (= P185), G190 (≠ T190), I192 (≠ L192), T194 (≠ A194), A196 (≠ F196)
Sites not aligning to the query:
P0AET8 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NAD-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.159 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 99% coverage: 1:249/252 of query aligns to 7:249/255 of P0AET8
- I23 (≠ F17) binding
- DI 42:43 (≠ DL 36:37) binding
- DI 68:69 (≠ NV 62:63) binding
- N95 (= N89) binding
- G99 (≠ T93) binding
- S146 (= S142) binding ; mutation S->A,H: Reduction of the catalytic efficiency by over 65%. No effect on the affinity for cholate and NAD.
- N151 (≠ R147) binding
- Y159 (= Y155) binding ; binding ; mutation to F: Loss of activity.; mutation to H: Reduction of the catalytic efficiency by 87.7%. No effect on the affinity for cholate and NAD.
- K163 (= K159) binding ; mutation to I: Reduction of the catalytic efficiency by 95%. No effect on the affinity for cholate and NAD.; mutation to R: Reduction of the catalytic efficiency by 35%. No effect on the affinity for cholate and NAD.
- ILT 192:194 (≠ LLA 192:194) binding
8hsaA Brucella melitensis 7-alpha-hydroxysteroid dehydrogenase mutant: 1-53 truncation/m196i/i258m/k262t-NAD+
40% identity, 99% coverage: 1:249/252 of query aligns to 3:245/248 of 8hsaA
- binding nicotinamide-adenine-dinucleotide: G14 (= G12), I19 (≠ F17), D38 (= D36), L39 (= L37), C63 (≠ G61), N64 (= N62), V65 (= V63), N91 (= N89), A92 (= A90), G93 (= G91), I140 (= I140), S141 (≠ A141), Y155 (= Y155), K159 (= K159), P185 (= P185), G186 (≠ V186)
7nm8AAA Antimycin pathway standalone ketoreductase, AntM (see paper)
39% identity, 99% coverage: 1:249/252 of query aligns to 2:247/251 of 7nm8AAA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), S15 (≠ G14), R16 (≠ S15), G17 (= G16), I18 (≠ F17), H36 (≠ N35), Y37 (vs. gap), G38 (≠ D36), H39 (≠ L37), L65 (≠ V63), N97 (= N89), G99 (= G91), S147 (= S142), Y160 (= Y155), K164 (= K159), G191 (≠ V186), T193 (≠ G188), T195 (= T190)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
37% identity, 99% coverage: 1:249/252 of query aligns to 1:243/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
37% identity, 97% coverage: 6:249/252 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 (≠ S15), I13 (≠ F17), N31 (= N35), Y32 (≠ D36), A33 (≠ L37), G34 (vs. gap), S35 (≠ N38), A58 (≠ G61), N59 (= N62), V60 (= V63), N86 (= N89), A87 (= A90), T109 (≠ V113), S138 (= S142), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (≠ E195)
7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
38% identity, 98% coverage: 3:249/252 of query aligns to 3:247/251 of 7djsD
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G16 (= G16), I17 (≠ F17), D36 (= D36), L37 (= L37), C61 (≠ G61), D62 (≠ N62), V63 (= V63), N89 (= N89), A90 (= A90), T140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), A186 (≠ V186), V187 (≠ I187)
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)
37% identity, 97% coverage: 6:249/252 of query aligns to 3:252/256 of Q48436
- 6:33 (vs. 9:36, 39% identical) binding
- D59 (≠ N62) binding
- K156 (= K159) binding
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
32% identity, 98% coverage: 3:249/252 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 (= S15), G16 (= G16), I17 (≠ F17), D36 (= D36), I37 (≠ L37), A61 (≠ G61), D62 (≠ N62), T63 (≠ V63), N89 (= N89), A90 (= A90), M140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), A186 (≠ V186), Y187 (≠ I187), I188 (≠ G188), L192 (= L192)
1gegE Cryatal structure analysis of meso-2,3-butanediol dehydrogenase (see paper)
37% identity, 97% coverage: 6:249/252 of query aligns to 3:252/256 of 1gegE
- active site: G13 (= G16), S139 (= S142), Y152 (= Y155), K156 (= K159), V197 (vs. gap)
- binding alpha-D-glucopyranose: R63 (= R66), D64 (≠ E67), F67 (≠ Q70), E123 (≠ P127)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), Q12 (≠ S15), I14 (≠ F17), D33 (= D36), Y34 (≠ L37), V58 (≠ G61), D59 (≠ N62), V60 (= V63), N86 (= N89), A87 (= A90), I109 (≠ V113), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), V185 (≠ G188), T187 (= T190), M189 (≠ L192)
Query Sequence
>BPHYT_RS05365 FitnessBrowser__BFirm:BPHYT_RS05365
MRLTGKTAIVTGGGSGFGEGIAKTYAREGANVVVNDLNGPAAERVASEIALAGGKAIAVT
GNVAQREDWQTLREAALEDFGSVQIVVNNAGTTHRNKPVMDVTEAEFDRVYAVNVKSIYW
SVQEFVPYFREQGGGCFINIASTAGVRPRPGLVWYNGSKGAVIIASKSLAVELGPDRIRV
NCVNPVIGETALLAEFMGVEDTPENRQRFLAGIPLGRFSTPQDIANAALYLASDEAEFIT
GVCLEVDGGRCV
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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