SitesBLAST
Comparing BWI76_RS16075 FitnessBrowser__Koxy:BWI76_RS16075 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)
4esoB Crystal structure of a putative oxidoreductase protein from sinorhizobium meliloti 1021 in complex with NADP
33% identity, 98% coverage: 4:243/246 of query aligns to 3:244/251 of 4esoB
- active site: G16 (= G17), S136 (= S136), M146 (≠ A146), Y149 (= Y149), K153 (= K153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), T14 (= T15), H15 (≠ S16), M17 (≠ I18), R37 (= R38), N38 (≠ D39), N41 (≠ R42), S58 (≠ N59), D59 (= D60), I60 (≠ A61), N86 (= N86), A87 (= A87), G88 (= G88), T134 (= T134), S136 (= S136), Y149 (= Y149), P179 (= P179), G180 (= G180), I182 (= I182), T184 (= T184), T186 (≠ F186), K187 (≠ R187), G188 (≠ H188)
4bmsF Short chain alcohol dehydrogenase from ralstonia sp. Dsm 6428 in complex with NADPH
35% identity, 99% coverage: 1:244/246 of query aligns to 1:247/249 of 4bmsF
- active site: S137 (= S136), H147 (≠ A146), Y150 (= Y149), K154 (= K153), Q195 (≠ D192)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), N15 (≠ T15), S16 (= S16), I18 (= I18), R38 (= R38), R39 (≠ D39), A59 (= A54), D60 (≠ R55), V61 (= V56), N87 (= N86), S88 (≠ A87), G89 (= G88), V110 (≠ T109), S137 (= S136), Y150 (= Y149), K154 (= K153), G181 (= G180), I183 (= I182), T185 (= T184), I187 (≠ F186)
6ihhA Crystal structure of rasadh f12 from ralstonia.Sp in complex with NADPH and a6o
35% identity, 99% coverage: 1:244/246 of query aligns to 1:247/249 of 6ihhA
- binding (2R,3S)-2-ethyl-2-[(2E)-2-(6-methoxy-3,4-dihydro-2H-naphthalen-1-ylidene)ethyl]-3-oxidanyl-cyclopentan-1-one: S137 (= S136), H147 (≠ A146), Y150 (= Y149), L188 (vs. gap), L246 (= L243)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), N15 (≠ T15), S16 (= S16), G17 (= G17), I18 (= I18), R38 (= R38), R39 (≠ D39), D60 (≠ R55), V61 (= V56), N87 (= N86), S88 (≠ A87), G89 (= G88), V110 (≠ T109), T135 (= T134), S137 (= S136), Y150 (= Y149), K154 (= K153), P180 (= P179), G181 (= G180), A182 (≠ P181), I183 (= I182), T185 (= T184), S187 (≠ F186)
5t2uA Short chain dehydrogenase/reductase family protein (see paper)
38% identity, 95% coverage: 10:242/246 of query aligns to 10:237/241 of 5t2uA
- active site: G17 (= G17), T135 (= T137), T145 (≠ A146), Y148 (= Y149), K152 (= K153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), G17 (= G17), R38 (= R38), D39 (= D39), R42 (= R42), D60 (= D60), L61 (≠ A61), N83 (= N86), A84 (= A87), Y87 (≠ A90), I133 (≠ A135), T135 (= T137), Y148 (= Y149), K152 (= K153), P178 (= P179), P180 (= P181), T181 (≠ I182), T183 (≠ H188), T185 (≠ M190), T186 (≠ R191)
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
38% identity, 72% coverage: 68:244/246 of query aligns to 71:251/253 of 4ituA
- active site: N113 (= N110), S141 (= S136), Y154 (= Y149), K158 (= K153)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S136), Y154 (= Y149), T186 (≠ P181), R209 (≠ V202), Y213 (≠ L206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: N89 (= N86), V112 (≠ T109), F139 (vs. gap), S141 (= S136), Y154 (= Y149), K158 (= K153), P184 (= P179), T186 (≠ P181), V187 (≠ I182), T190 (≠ D185), M192 (vs. gap)
Sites not aligning to the query:
A7IQH5 2-(S)-hydroxypropyl-CoM dehydrogenase 3; S-HPCDH 3; 2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3; Aliphatic epoxide carboxylation component IV; Epoxide carboxylase component IV; SHPCDH3; EC 1.1.1.269 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 2 papers)
38% identity, 72% coverage: 68:244/246 of query aligns to 73:253/255 of A7IQH5
- N91 (= N86) binding
- S143 (= S136) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y149) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K153) binding ; mutation to A: Loss of activity.
- T188 (≠ P181) binding
- VTSTG 189:193 (≠ IDTDF 182:186) binding
- R211 (≠ V202) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- K214 (≠ R205) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- Y215 (≠ L206) binding
Sites not aligning to the query:
- 19 binding
- 38 binding
- 64:65 binding
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
39% identity, 72% coverage: 68:244/246 of query aligns to 71:246/248 of 4gh5A
- active site: N113 (= N110), S141 (= S136), Y154 (= Y149), K158 (= K153)
- binding nicotinamide-adenine-dinucleotide: N89 (= N86), A90 (= A87), V112 (≠ T109), F139 (vs. gap), S141 (= S136), Y154 (= Y149), K158 (= K153), P184 (= P179), V187 (≠ I182), T190 (≠ D185), G191 (≠ F186), M192 (= M190)
Sites not aligning to the query:
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
30% identity, 99% coverage: 1:244/246 of query aligns to 2:253/255 of 5itvA
- active site: G18 (= G17), S141 (= S136), Y154 (= Y149), K158 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), D38 (≠ T36), I39 (≠ G37), T61 (≠ N59), I63 (≠ A61), N89 (= N86), G91 (= G88), T139 (= T134), S141 (= S136), Y154 (= Y149), K158 (= K153), P184 (= P179), G185 (= G180), I186 (≠ P181), I187 (= I182)
2zatA Crystal structure of a mammalian reductase (see paper)
33% identity, 96% coverage: 7:242/246 of query aligns to 6:246/251 of 2zatA
- active site: G16 (= G17), S142 (= S136), L152 (≠ A146), Y155 (= Y149), K159 (= K153), K200 (≠ E193)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G13), T14 (= T15), D15 (≠ S16), G16 (= G17), I17 (= I18), S36 (≠ G37), R37 (= R38), K38 (≠ D39), N41 (vs. gap), H62 (≠ D58), N89 (= N86), A91 (≠ G88), V140 (≠ T134), S142 (= S136), Y155 (= Y149), K159 (= K153), P185 (= P179), G186 (= G180), I188 (= I182), T190 (= T184), F192 (= F186), S193 (≠ R187)
Q8WNV7 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; PHCR; NADPH-dependent retinol dehydrogenase/reductase; NDRD; Peroxisomal carbonyl reductase; PerCR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; EC 1.1.1.184; EC 1.1.1.300 from Sus scrofa (Pig) (see 2 papers)
33% identity, 96% coverage: 7:242/246 of query aligns to 34:274/279 of Q8WNV7
- 37:61 (vs. 10:34, 48% identical) binding
- F177 (≠ A143) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to S: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with F-180.
- L180 (≠ A146) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to F: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with S-177.
- Y183 (= Y149) active site, Proton acceptor
- K187 (= K153) binding
- N196 (≠ C162) Important for the maintenance of the quaternary structure, the catalytic activity and cold stability
Sites not aligning to the query:
- 277:279 Peroxisomal targeting signal
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
31% identity, 98% coverage: 7:246/246 of query aligns to 9:253/254 of 3o4rA
- active site: G19 (= G17), S145 (= S136), F155 (≠ A146), Y158 (= Y149), K162 (= K153), K203 (≠ R196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G13), T17 (= T15), D18 (≠ S16), G19 (= G17), I20 (= I18), S39 (≠ G37), R40 (= R38), K41 (≠ D39), N44 (≠ R42), H65 (≠ D58), V66 (vs. gap), N92 (= N86), A94 (≠ G88), S145 (= S136), Y158 (= Y149), K162 (= K153), P188 (= P179), G189 (= G180), L190 (≠ P181), I191 (= I182), T193 (= T184), F195 (= F186), S196 (≠ R187)
Q9BTZ2 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; NADPH-dependent retinol dehydrogenase/reductase; NRDR; humNRDR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; SCAD-SRL; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; Short-chain dehydrogenase/reductase family member 4; EC 1.1.1.184 from Homo sapiens (Human) (see 2 papers)
31% identity, 98% coverage: 7:246/246 of query aligns to 33:277/278 of Q9BTZ2
- S176 (≠ A143) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.
- F179 (≠ A146) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.
- T195 (≠ C162) mutation to N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.
D4A1J4 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Rattus norvegicus (Rat) (see paper)
30% identity, 100% coverage: 1:245/246 of query aligns to 1:245/245 of D4A1J4
- Y147 (= Y149) mutation to F: Loss of function.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
32% identity, 98% coverage: 3:244/246 of query aligns to 2:242/251 of 6xewA
- active site: G16 (= G17), S138 (= S136), Y151 (= Y149)
- binding r,3-hydroxybutan-2-one: S138 (= S136), S140 (= S138), Y151 (= Y149)
- binding s,3-hydroxybutan-2-one: S138 (= S136), Y151 (= Y149), S182 (≠ G180)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ S16), G16 (= G17), M17 (≠ I18), D36 (≠ G37), W37 (≠ R38), W37 (≠ R38), A38 (≠ D39), I59 (≠ N59), D60 (= D60), V61 (≠ A61), N87 (= N86), A88 (= A87), G89 (= G88), V110 (≠ T109), T136 (= T134), S138 (= S136), Y151 (= Y149), K155 (= K153), S182 (≠ G180), L183 (≠ P181), V184 (≠ I182), T186 (= T184), N187 (≠ D185), M188 (≠ F186), T189 (≠ R187)
3toxA Crystal structure of a short chain dehydrogenase in complex with NAD(p) from sinorhizobium meliloti 1021
35% identity, 98% coverage: 2:242/246 of query aligns to 1:249/254 of 3toxA
- active site: G16 (= G17), S142 (= S136), V153 (≠ A146), Y156 (= Y149), K160 (= K153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (≠ T15), S15 (= S16), G16 (= G17), I17 (= I18), A36 (≠ G37), R37 (= R38), N38 (≠ D39), V63 (vs. gap), N89 (= N86), A90 (= A87), G91 (= G88), T140 (= T134), S142 (= S136), Y156 (= Y149), K160 (= K153), P186 (= P179), G188 (≠ P181), T189 (≠ I182), T191 (= T184)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
32% identity, 98% coverage: 3:244/246 of query aligns to 2:242/251 of 6vspA
- active site: G16 (= G17), S138 (= S136), Y151 (= Y149)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ S16), G16 (= G17), M17 (≠ I18), D36 (≠ G37), W37 (≠ R38), W37 (≠ R38), A38 (≠ D39), I59 (≠ N59), D60 (= D60), V61 (≠ A61), N87 (= N86), A88 (= A87), G89 (= G88), V90 (≠ Y89), V110 (≠ T109), T136 (= T134), S138 (= S136), Y151 (= Y149), K155 (= K153), P181 (= P179), S182 (≠ G180), L183 (≠ P181), V184 (≠ I182), T186 (= T184), N187 (≠ D185), M188 (≠ F186), T189 (≠ R187)
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)
32% identity, 98% coverage: 3:244/246 of query aligns to 2:242/251 of H9XP47
- N15 (≠ S16) binding
- M17 (≠ I18) binding
- D36 (≠ G37) binding
- D60 (= D60) binding
- V61 (≠ A61) binding
- N87 (= N86) binding
- S138 (= S136) binding ; binding
- V139 (≠ T137) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (= S138) binding
- Y151 (= Y149) binding ; binding ; binding
- K155 (= K153) binding
- V184 (≠ I182) binding
- T186 (= T184) binding
- RDK 197:199 (≠ RRE 195:197) 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.
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
32% identity, 98% coverage: 3:244/246 of query aligns to 4:244/252 of 6vspB
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
33% identity, 96% coverage: 7:243/246 of query aligns to 6:251/256 of 7do7A
- active site: G16 (= G17), S146 (= S136), Y159 (= Y149)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), R15 (≠ S16), G16 (= G17), I17 (= I18), S37 (≠ T36), D66 (= D60), A67 (= A61), N93 (= N86), A94 (= A87), G95 (= G88), I96 (≠ Y89), V144 (≠ T134), S145 (≠ A135), S146 (= S136), Y159 (= Y149), K163 (= K153), P189 (= P179), G190 (= G180), I192 (= I182), T194 (= T184), I196 (≠ F186)
- binding beta-L-rhamnopyranose: F99 (≠ V92), S146 (= S136), S148 (= S138), Q156 (≠ A146), Y159 (= Y149), N197 (vs. gap), D235 (= D227), M236 (≠ A228), R238 (≠ S230)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
33% identity, 96% coverage: 7:243/246 of query aligns to 6:251/256 of 7b81A
- active site: G16 (= G17), S146 (= S136), Y159 (= Y149)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S14 (≠ T15), R15 (≠ S16), I17 (= I18), D66 (= D60), A67 (= A61), N93 (= N86), A94 (= A87), G95 (= G88), I96 (≠ Y89), T116 (= T109), V144 (≠ T134), S146 (= S136), Y159 (= Y149), K163 (= K153), P189 (= P179), G190 (= G180), I192 (= I182), T194 (= T184), I196 (≠ F186)
Query Sequence
>BWI76_RS16075 FitnessBrowser__Koxy:BWI76_RS16075
MARFSAKRVLITGATSGIGLAGAQRIDREGGWVIATGRDPRRLALLRRQLSDRARVIDND
ASDPLTGAALAKEIHASGGLDGLWLNAGYAAVGELSQIDAAAFDHMMATNVRGPVLQMAA
LAGKLNPGASVVVTASTSAYEGAAAASLYSATKGALISLTRCWASALGEKNIRVNALVPG
PIDTDFRHFMRDEARREFEASVVSRLALHRQGTAAEAAEVALFLLSDAASFVSGGQYAVD
GGLTLR
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