SitesBLAST
Comparing PfGW456L13_3453 Short-chain dehydrogenase/reductase SDR 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)
G9FRD7 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NADP-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.- from Clostridium sardiniense (Clostridium absonum) (see 2 papers)
38% identity, 93% coverage: 5:257/272 of query aligns to 1:254/262 of G9FRD7
- SSTRGI 13:18 (≠ GAGSGI 17:22) binding
- R38 (≠ L42) binding ; mutation to D: Loss of catalytic activity.
- NA 63:64 (≠ DV 64:65) binding
- N90 (= N91) binding
- T145 (≠ S148) binding
- Y158 (= Y161) binding ; binding
- K162 (= K165) binding
- IGTRA 191:195 (≠ IRTPA 194:198) binding
Sites not aligning to the query:
- 261:262 mutation Missing: 5-fold reduction in catalytic efficiency.
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
38% identity, 94% coverage: 3:258/272 of query aligns to 3:258/258 of 4wecA
- active site: G21 (= G21), S143 (= S148), Q154 (= Q158), Y157 (= Y161), K161 (= K165)
- binding nicotinamide-adenine-dinucleotide: G17 (= G17), A19 (≠ G19), S20 (= S20), G21 (= G21), I22 (= I22), D41 (= D41), I42 (≠ L42), V61 (= V63), D62 (= D64), V63 (= V65), N89 (= N91), T141 (= T146), Y157 (= Y161), K161 (= K165), P187 (= P191), P189 (≠ V193), V190 (≠ I194)
5epoA The three-dimensional structure of clostridium absonum 7alpha- hydroxysteroid dehydrogenase (see paper)
38% identity, 93% coverage: 6:257/272 of query aligns to 1:253/261 of 5epoA
- active site: G16 (= G21), T144 (≠ S148), I152 (= I156), Y157 (= Y161), K161 (= K165), R193 (≠ P197)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S12 (≠ G17), T14 (≠ G19), R15 (≠ S20), G16 (= G21), I17 (= I22), R37 (≠ L42), F61 (≠ V63), N62 (≠ D64), N89 (= N91), Y90 (= Y94), G91 (≠ R95), Y157 (= Y161), K161 (= K165), P187 (= P191), G188 (= G192), I190 (= I194), T192 (= T196), R193 (≠ P197), A194 (= A198), A195 (≠ M199)
- binding taurochenodeoxycholic acid: T93 (≠ P97), T144 (≠ S148), G146 (≠ S150), R154 (≠ Q158), Y157 (= Y161), G188 (= G192), N198 (≠ W202), M199 (≠ A203), F203 (≠ M207)
Q8JZV9 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 Mus musculus (Mouse) (see paper)
39% identity, 91% coverage: 7:253/272 of query aligns to 3:244/245 of Q8JZV9
- Y147 (= Y161) active site, Proton acceptor; mutation to F: Loss of function.
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)
39% identity, 91% coverage: 7:253/272 of query aligns to 3:244/245 of D4A1J4
- Y147 (= Y161) mutation to F: Loss of function.
4nbuB Crystal structure of fabg from bacillus sp (see paper)
38% identity, 91% coverage: 5:252/272 of query aligns to 2:242/244 of 4nbuB
- active site: G18 (= G21), N111 (= N120), S139 (= S148), Q149 (= Q158), Y152 (= Y161), K156 (= K165)
- binding acetoacetyl-coenzyme a: D93 (= D102), K98 (≠ N107), S139 (= S148), N146 (≠ E155), V147 (≠ I156), Q149 (= Q158), Y152 (= Y161), F184 (≠ V193), M189 (= M199), K200 (≠ A210)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G17), N17 (≠ S20), G18 (= G21), I19 (= I22), D38 (= D41), F39 (= F43), V59 (= V63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (≠ A98), I90 (≠ T99), T137 (= T146), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), F184 (≠ V193), T185 (≠ I194), T187 (= T196), M189 (= M199)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
36% identity, 93% coverage: 7:259/272 of query aligns to 4:252/252 of 6vspB
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
36% identity, 93% coverage: 7:259/272 of query aligns to 2:250/251 of 6vspA
- active site: G16 (= G21), S138 (= S148), Y151 (= Y161)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), N15 (≠ S20), G16 (= G21), M17 (≠ I22), D36 (= D41), W37 (≠ L42), W37 (≠ L42), A38 (≠ F43), I59 (≠ V63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (≠ V93), V90 (≠ Y94), V110 (= V119), T136 (= T146), S138 (= S148), Y151 (= Y161), K155 (= K165), P181 (= P191), S182 (≠ G192), L183 (≠ V193), V184 (≠ I194), T186 (= T196), N187 (≠ P197), M188 (≠ A198), T189 (≠ M199)
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)
36% identity, 93% coverage: 7:259/272 of query aligns to 2:250/251 of H9XP47
- N15 (≠ S20) binding
- M17 (≠ I22) binding
- D36 (= D41) binding
- D60 (= D64) binding
- V61 (= V65) binding
- N87 (= N91) binding
- S138 (= S148) binding ; binding
- V139 (≠ T149) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (= S150) binding
- Y151 (= Y161) binding ; binding ; binding
- K155 (= K165) binding
- V184 (≠ I194) binding
- T186 (= T196) binding
- RDK 197:199 (≠ KSA 208:210) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
- Q247 (≠ T256) mutation to 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)
36% identity, 93% coverage: 7:259/272 of query aligns to 2:250/251 of 6xewA
- active site: G16 (= G21), S138 (= S148), Y151 (= Y161)
- binding r,3-hydroxybutan-2-one: S138 (= S148), S140 (= S150), Y151 (= Y161)
- binding s,3-hydroxybutan-2-one: S138 (= S148), Y151 (= Y161), S182 (≠ G192)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), N15 (≠ S20), G16 (= G21), M17 (≠ I22), D36 (= D41), W37 (≠ L42), W37 (≠ L42), A38 (≠ F43), I59 (≠ V63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (≠ V93), V110 (= V119), T136 (= T146), S138 (= S148), Y151 (= Y161), K155 (= K165), S182 (≠ G192), L183 (≠ V193), V184 (≠ I194), T186 (= T196), N187 (≠ P197), M188 (≠ A198), T189 (≠ M199)
3toxA Crystal structure of a short chain dehydrogenase in complex with NAD(p) from sinorhizobium meliloti 1021
40% identity, 92% coverage: 6:254/272 of query aligns to 1:252/254 of 3toxA
- active site: G16 (= G21), S142 (= S148), V153 (≠ Q158), Y156 (= Y161), K160 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G17), S14 (≠ G19), S15 (= S20), G16 (= G21), I17 (= I22), A36 (≠ D41), R37 (≠ L42), N38 (≠ F43), V63 (= V65), N89 (= N91), A90 (= A92), G91 (≠ P97), T140 (= T146), S142 (= S148), Y156 (= Y161), K160 (= K165), P186 (= P191), G188 (≠ V193), T189 (≠ I194), T191 (= T196)
Q5P5I4 (S)-1-Phenylethanol dehydrogenase; EC 1.1.1.311 from Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) (see 2 papers)
38% identity, 91% coverage: 6:252/272 of query aligns to 3:246/249 of Q5P5I4
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2ewmB Crystal structure of the (s)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain ebn1 (see paper)
38% identity, 91% coverage: 6:252/272 of query aligns to 1:244/247 of 2ewmB
- active site: G16 (= G21), S139 (= S148), Y149 (≠ Q158), Y152 (= Y161), K156 (= K165)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), N15 (≠ S20), G16 (= G21), I17 (= I22), D36 (= D41), L37 (= L42), C59 (≠ V63), D60 (= D64), V61 (= V65), N87 (= N91), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), S183 (≠ G192), L184 (≠ V193), V185 (≠ I194), T189 (≠ A198)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
32% identity, 90% coverage: 8:253/272 of query aligns to 3:246/248 of 6ixmC
- active site: G16 (= G21), S142 (= S148), Y155 (= Y161), K159 (= K165)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), S15 (= S20), G16 (= G21), I17 (= I22), D36 (= D41), I37 (≠ L42), A61 (≠ V63), D62 (= D64), T63 (≠ V65), N89 (= N91), A90 (= A92), M140 (≠ T146), S142 (= S148), Y155 (= Y161), K159 (= K165), P185 (= P191), A186 (≠ G192), Y187 (≠ V193), I188 (= I194), L192 (≠ A198)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
34% identity, 92% coverage: 6:254/272 of query aligns to 3:253/254 of 4fn4A
- active site: G18 (= G21), S144 (= S148), Y157 (= Y161), K161 (= K165), S202 (≠ A203)
- binding nicotinamide-adenine-dinucleotide: G14 (= G17), S17 (= S20), G18 (= G21), I19 (= I22), E38 (≠ D41), L39 (= L42), R43 (≠ S46), A63 (≠ V63), D64 (= D64), V65 (= V65), N91 (= N91), G93 (≠ V93), I94 (≠ Y94), T142 (= T146), S144 (= S148), Y157 (= Y161), K161 (= K165), P187 (= P191), V190 (≠ I194), T192 (= T196), N193 (≠ P197), I194 (vs. gap)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
34% identity, 92% coverage: 4:253/272 of query aligns to 1:251/261 of P40288
- 11:35 (vs. 14:38, 56% identical) binding
- E96 (≠ R95) mutation E->A,G,K: Heat stable.
- D108 (≠ N107) mutation to N: Heat stable.
- V112 (≠ C116) mutation to A: Heat stable.
- E133 (≠ A137) mutation to K: Heat stable.
- V183 (≠ C186) mutation to I: Heat stable.
- P194 (= P197) mutation to Q: Heat stable.
- E210 (≠ L212) mutation to K: Heat stable.
- Y217 (≠ Q219) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
37% identity, 91% coverage: 7:254/272 of query aligns to 10:265/267 of Q9LBG2
- 17:42 (vs. 14:39, 58% identical) binding
- E103 (vs. gap) 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)
37% identity, 91% coverage: 7:254/272 of query aligns to 1:256/258 of 1iy8A
- active site: G15 (= G21), S143 (= S148), Q153 (= Q158), Y156 (= Y161), K160 (= K165)
- binding nicotinamide-adenine-dinucleotide: G11 (= G17), S14 (= S20), G15 (= G21), L16 (≠ I22), D35 (= D41), V36 (≠ L42), A62 (vs. gap), D63 (= D64), V64 (= V65), N90 (= N91), G92 (≠ V93), I93 (vs. gap), T141 (= T146), S143 (= S148), Y156 (= Y161), K160 (= K165), P186 (= P191), G187 (= G192), T191 (= T196), P192 (= P197), M193 (≠ A198)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
34% identity, 92% coverage: 4:253/272 of query aligns to 1:251/261 of 1g6kA
- active site: G18 (= G21), S145 (= S148), Y158 (= Y161), K162 (= K165)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S20), G18 (= G21), L19 (≠ I22), R39 (≠ L42), D65 (= D64), V66 (= V65), N92 (= N91), A93 (= A92), G94 (≠ V93), M143 (≠ T146), S145 (= S148), Y158 (= Y161), P188 (= P191), G189 (= G192), I191 (= I194), T193 (= T196)
2ag5A Crystal structure of human dhrs6 (see paper)
36% identity, 92% coverage: 7:255/272 of query aligns to 3:246/246 of 2ag5A
- active site: S133 (= S148), Y147 (= Y161), K151 (= K165), R192 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: Q16 (≠ S20), G17 (= G21), I18 (= I22), D37 (= D41), I38 (≠ L42), D58 (≠ Q62), V59 (= V63), V81 (≠ N91), G83 (≠ V93), L104 (≠ V119), Y147 (= Y161), K151 (= K165), P177 (= P191), V180 (≠ I194), T182 (= T196), S184 (≠ A198)
- binding sulfate ion: R144 (≠ Q158), R188 (≠ W202), F202 (= F211), R205 (≠ L214)
Query Sequence
>PfGW456L13_3453 Short-chain dehydrogenase/reductase SDR
MSEILKRLDGKVCVITGAGSGIGRASALRFAREGATVVVTDLFAESAQAVAAEIGVNALV
LQVDVGQEDALREMVEQTVRTFGRIDVLFNNAVYRNPATTRDIDFINFNTELFHNCMRVN
VLGGVLACKYALPHMLAQGSGSILFTSSTSSIAGEISQFSYGASKAALNWYVQTIAATFG
KRGIRCNGILPGVIRTPAMESWANEAMKSAFLDLQNVPQLGEPEDIAAMAAFLASDDAAY
VNGTLMRVDGGMSCGTPMVPVVRNFLLPQASI
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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