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Comparing BPHYT_RS16940 FitnessBrowser__BFirm:BPHYT_RS16940 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)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
40% identity, 98% coverage: 4:255/258 of query aligns to 3:248/248 of 6ixmC
- active site: G16 (= G17), S142 (= S143), Y155 (= Y156), K159 (= K160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (≠ R16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), A61 (≠ T63), D62 (= D64), T63 (≠ V65), N89 (= N91), A90 (= A92), M140 (≠ I141), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (= P186), A186 (≠ G187), Y187 (= Y188), I188 (= I189), L192 (= L193)
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
39% identity, 96% coverage: 4:251/258 of query aligns to 3:244/248 of 4urfB
- active site: G16 (= G17), S142 (= S143), I152 (≠ C153), Y155 (= Y156), K159 (= K160)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ M217), R211 (≠ K218), R212 (= R219)
- binding bicarbonate ion: I92 (= I94), G94 (vs. gap), R109 (= R110), R179 (= R180), S228 (= S235)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (= G15), N15 (≠ R16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), D62 (= D64), T63 (≠ V65), N89 (= N91), A90 (= A92), G91 (= G93), I140 (= I141), Y155 (= Y156), K159 (= K160), P185 (= P186), A186 (≠ G187), I188 (= I189), T190 (= T191)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
39% identity, 96% coverage: 4:251/258 of query aligns to 3:244/248 of 4urfA
- active site: G16 (= G17), S142 (= S143), I152 (≠ C153), Y155 (= Y156), K159 (= K160)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (= I94), S93 (≠ N95), G94 (vs. gap), E95 (≠ V96), T97 (≠ C98), E101 (≠ T102), T103 (= T104), Q106 (≠ D107), R109 (= R110), S175 (≠ P176), G177 (≠ N178)
- binding magnesium ion: S237 (≠ T244), Y238 (≠ C245)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (= G15), N15 (≠ R16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), W41 (≠ T42), D62 (= D64), T63 (≠ V65), N89 (= N91), A90 (= A92), G91 (= G93), I140 (= I141), Y155 (= Y156), K159 (= K160), P185 (= P186), I188 (= I189), T190 (= T191)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
39% identity, 96% coverage: 4:251/258 of query aligns to 3:244/248 of 4ureB
- active site: G16 (= G17), S142 (= S143), I152 (≠ C153), Y155 (= Y156), K159 (= K160)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ R16), G16 (= G17), I17 (= I18), N89 (= N91), G91 (= G93), Y155 (= Y156), P185 (= P186), A186 (≠ G187)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
35% identity, 98% coverage: 3:254/258 of query aligns to 4:254/255 of 5itvA
- active site: G18 (= G17), S141 (= S143), Y154 (= Y156), K158 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (≠ R16), G18 (= G17), I19 (= I18), D38 (≠ E37), I39 (≠ L38), T61 (= T63), I63 (≠ V65), N89 (= N91), G91 (= G93), T139 (≠ I141), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (= P186), G185 (= G187), I186 (≠ Y188), I187 (= I189)
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)
39% identity, 98% coverage: 3:254/258 of query aligns to 2:243/251 of H9XP47
- N15 (≠ R16) binding
- M17 (≠ I18) binding
- D36 (≠ E37) binding
- D60 (= D64) binding
- V61 (= V65) binding
- N87 (= N91) binding
- S138 (= S143) binding ; binding
- V139 (≠ T144) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ H145) binding
- Y151 (= Y156) binding ; binding ; binding
- K155 (= K160) binding
- V184 (≠ I189) binding
- T186 (= T191) binding
- RDK 197:199 (≠ ADP 202:204) 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.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
39% identity, 98% coverage: 3:254/258 of query aligns to 2:243/251 of 6xewA
- active site: G16 (= G17), S138 (= S143), Y151 (= Y156)
- binding r,3-hydroxybutan-2-one: S138 (= S143), S140 (≠ H145), Y151 (= Y156)
- binding s,3-hydroxybutan-2-one: S138 (= S143), Y151 (= Y156), S182 (≠ G187)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ R16), G16 (= G17), M17 (≠ I18), D36 (≠ E37), W37 (≠ L38), W37 (≠ L38), A38 (≠ D39), I59 (≠ T63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (= G93), V110 (= V114), T136 (≠ I141), S138 (= S143), Y151 (= Y156), K155 (= K160), S182 (≠ G187), L183 (≠ Y188), V184 (≠ I189), T186 (= T191), N187 (≠ Q192), M188 (≠ L193), T189 (= T194)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
39% identity, 98% coverage: 3:254/258 of query aligns to 4:245/252 of 6vspB
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
39% identity, 98% coverage: 3:254/258 of query aligns to 2:243/251 of 6vspA
- active site: G16 (= G17), S138 (= S143), Y151 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ R16), G16 (= G17), M17 (≠ I18), D36 (≠ E37), W37 (≠ L38), W37 (≠ L38), A38 (≠ D39), I59 (≠ T63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (= G93), V90 (≠ I94), V110 (= V114), T136 (≠ I141), S138 (= S143), Y151 (= Y156), K155 (= K160), P181 (= P186), S182 (≠ G187), L183 (≠ Y188), V184 (≠ I189), T186 (= T191), N187 (≠ Q192), M188 (≠ L193), T189 (= T194)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
37% identity, 98% coverage: 2:255/258 of query aligns to 3:254/254 of 4fn4A
- active site: G18 (= G17), S144 (= S143), Y157 (= Y156), K161 (= K160), S202 (≠ D203)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (≠ R16), G18 (= G17), I19 (= I18), E38 (= E37), L39 (= L38), R43 (≠ T42), A63 (≠ T63), D64 (= D64), V65 (= V65), N91 (= N91), G93 (= G93), I94 (= I94), T142 (≠ I141), S144 (= S143), Y157 (= Y156), K161 (= K160), P187 (= P186), V190 (≠ I189), T192 (= T191), N193 (≠ Q192), I194 (≠ L193)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
38% identity, 99% coverage: 2:256/258 of query aligns to 6:254/258 of 4wecA
- active site: G21 (= G17), S143 (= S146), Q154 (vs. gap), Y157 (= Y156), K161 (= K160)
- binding nicotinamide-adenine-dinucleotide: G17 (= G13), A19 (≠ G15), S20 (≠ R16), G21 (= G17), I22 (= I18), D41 (≠ E37), I42 (≠ L38), V61 (≠ T63), D62 (= D64), V63 (= V65), N89 (= N91), T141 (= T144), Y157 (= Y156), K161 (= K160), P187 (= P186), P189 (≠ Y188), V190 (≠ I189)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
39% identity, 96% coverage: 7:253/258 of query aligns to 5:243/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), M16 (≠ I18), D35 (≠ E37), I36 (≠ L38), I62 (≠ V65), N88 (= N91), G90 (= G93), I138 (= I141), S140 (= S143), Y152 (= Y156), K156 (= K160), I185 (= I189)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 97% coverage: 1:251/258 of query aligns to 2:241/244 of 4nbuB
- active site: G18 (= G17), N111 (≠ D115), S139 (= S143), Q149 (≠ C153), Y152 (= Y156), K156 (= K160)
- binding acetoacetyl-coenzyme a: D93 (≠ F97), K98 (≠ T102), S139 (= S143), N146 (≠ I150), V147 (≠ P151), Q149 (≠ C153), Y152 (= Y156), F184 (≠ Y188), M189 (≠ L193), K200 (≠ P204)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ R16), G18 (= G17), I19 (= I18), D38 (≠ E37), F39 (≠ L38), V59 (≠ T63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (= G93), I90 (= I94), T137 (≠ I141), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), F184 (≠ Y188), T185 (≠ I189), T187 (= T191), M189 (≠ L193)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
39% identity, 96% coverage: 7:253/258 of query aligns to 6:244/248 of Q9KJF1
- S15 (≠ R16) binding
- D36 (≠ E37) binding
- D62 (= D64) binding
- I63 (≠ V65) binding
- N89 (= N91) binding
- Y153 (= Y156) binding
- K157 (= K160) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
39% identity, 97% coverage: 1:251/258 of query aligns to 6:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G13), S20 (≠ G15), K21 (≠ R16), G22 (= G17), I23 (= I18), A43 (≠ L38), S44 (≠ D39), S45 (≠ I40), G68 (≠ T63), D69 (= D64), V70 (= V65), N96 (= N91), S97 (≠ A92), G98 (= G93), Y100 (≠ N95), I144 (= I141), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (= G187), M191 (≠ Y188), I192 (= I189), T194 (= T191), G196 (≠ L193), T197 (= T194)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (= Y156), M191 (≠ Y188), I202 (≠ N199)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
36% identity, 98% coverage: 3:256/258 of query aligns to 10:267/267 of Q9LBG2
- 17:42 (vs. 10:35, 50% identical) binding
- E103 (≠ N95) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
1iy8A Crystal structure of levodione reductase (see paper)
36% identity, 98% coverage: 3:256/258 of query aligns to 1:258/258 of 1iy8A
- active site: G15 (= G17), S143 (= S143), Q153 (≠ C153), Y156 (= Y156), K160 (= K160)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), S14 (≠ R16), G15 (= G17), L16 (≠ I18), D35 (≠ E37), V36 (≠ L38), A62 (≠ T63), D63 (= D64), V64 (= V65), N90 (= N91), G92 (= G93), I93 (= I94), T141 (≠ I141), S143 (= S143), Y156 (= Y156), K160 (= K160), P186 (= P186), G187 (= G187), T191 (= T191), P192 (≠ Q192), M193 (≠ L193)
2ztlA Closed conformation of d-3-hydroxybutyrate dehydrogenase complexed with NAD+ and l-3-hydroxybutyrate (see paper)
38% identity, 97% coverage: 4:254/258 of query aligns to 2:259/260 of 2ztlA
- active site: G15 (= G17), N114 (≠ D115), S142 (= S143), Y155 (= Y156), K159 (= K160), L200 (≠ Q201)
- binding (3s)-3-hydroxybutanoic acid: Q94 (≠ N95), S142 (= S143), H144 (= H145), K152 (≠ C153), Y155 (= Y156), Q196 (≠ W197)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), G15 (= G17), I16 (= I18), F36 (≠ L38), L64 (≠ V65), N90 (= N91), A91 (= A92), G92 (= G93), L113 (≠ V114), Y155 (= Y156), K159 (= K160), P185 (= P186), W187 (≠ Y188), V188 (≠ I189), T190 (= T191), V193 (≠ T194)
1wmbA Crystal structure of NAD dependent d-3-hydroxybutylate dehydrogenase (see paper)
38% identity, 97% coverage: 4:254/258 of query aligns to 2:259/260 of 1wmbA
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
35% identity, 98% coverage: 2:254/258 of query aligns to 3:260/261 of 6zzsD
- active site: G18 (= G17), S143 (= S143), Y156 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (≠ R16), I19 (= I18), D38 (≠ E37), M39 (≠ L38), D64 (= D64), V65 (= V65), N91 (= N91), A92 (= A92), G93 (= G93), M141 (≠ I141), A142 (= A142), S143 (= S143), Y156 (= Y156), K160 (= K160), P186 (= P186), G187 (= G187), V189 (≠ I189), T191 (= T191), L193 (= L193)
- binding 3-oxidanylidenepentanoic acid: Q95 (≠ N95), S143 (= S143), N145 (≠ H145), K153 (≠ C153), Y156 (= Y156), Q197 (≠ E200)
Query Sequence
>BPHYT_RS16940 FitnessBrowser__BFirm:BPHYT_RS16940
MKRLAGKVALVTGAGRGIGSAIAHAFAREGAAVVLAELDIETARQTAEHIKAQTGARVLA
VHTDVTQSASVQHAVSEAERAFGALDVLVNNAGINVFCDPLTMTDDDWRRCFAVDLDGVW
NGCRAALPGMVERGAGSIVNIASTHSFKIIPGCFPYPVAKHGVIGLTRALGIEYAPRNVR
VNAIAPGYIETQLTHDWWNEQADPAAAQQATLDLQPMKRIGRPEEVAMTAVFLASDEAPF
INATCITVDGGRSALYHD
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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