SitesBLAST
Comparing 3608297 Dshi_1700 short-chain dehydrogenase/reductase SDR (RefSeq) 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)
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
56% identity, 100% coverage: 1:250/251 of query aligns to 7:258/261 of 4o5oB
Sites not aligning to the query:
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
56% identity, 100% coverage: 1:250/251 of query aligns to 4:252/255 of 4xgnA
- active site: Y161 (= Y159), K165 (= K163)
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (≠ R37), C59 (≠ T56), D60 (= D57), V61 (= V58), C86 (= C84), A87 (= A85), V113 (≠ I111), T146 (= T144), Y161 (= Y159), K165 (= K163), P191 (= P189), I193 (= I191), F194 (= F192), T196 (= T194), M198 (= M196)
O18404 3-hydroxyacyl-CoA dehydrogenase type-2; 17-beta-hydroxysteroid dehydrogenase 10; 17-beta-HSD 10; 3-hydroxyacyl-CoA dehydrogenase type II; Hydroxysteroid dehydrogenase; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Scully protein; Type II HADH; EC 1.1.1.35; EC 1.1.1.51; EC 1.1.1.62; EC 1.1.1.-; EC 1.1.1.53 from Drosophila melanogaster (Fruit fly) (see paper)
52% identity, 96% coverage: 9:250/251 of query aligns to 8:253/255 of O18404
- L33 (≠ V34) mutation to Q: Lethal allele.
- F120 (= F117) mutation to I: Lethal allele.
7onuC Structure of human mitochondrial rnase p in complex with mitochondrial pre-tRNA-tyr (see paper)
51% identity, 96% coverage: 9:250/251 of query aligns to 8:253/255 of 7onuC
- binding nicotinamide-adenine-dinucleotide: S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (≠ R37), V59 (= V58), C85 (= C84), S149 (= S146), Y162 (= Y159), F195 (= F192), T197 (= T194)
- binding : S92 (≠ A91), K93 (= K92)
Q99714 3-hydroxyacyl-CoA dehydrogenase type-2; 17-beta-estradiol 17-dehydrogenase; 2-methyl-3-hydroxybutyryl-CoA dehydrogenase; MHBD; 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)); 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase type II; 3alpha(or 20beta)-hydroxysteroid dehydrogenase; 7-alpha-hydroxysteroid dehydrogenase; Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Short chain dehydrogenase/reductase family 5C member 1; Short-chain type dehydrogenase/reductase XH98G2; Type II HADH; EC 1.1.1.35; EC 1.1.1.62; EC 1.1.1.239; EC 1.1.1.178; EC 1.1.1.53; EC 1.1.1.159 from Homo sapiens (Human) (see 14 papers)
51% identity, 96% coverage: 9:250/251 of query aligns to 14:259/261 of Q99714
- S20 (= S15) binding ; mutation to F: Decreased dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation.
- L22 (= L17) binding
- D41 (= D36) binding
- D64 (= D57) binding
- V65 (= V58) binding ; to A: in HSD10MD; uncertain significance; dbSNP:rs104886492
- D86 (≠ T79) to G: in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; no effect on NAD(+) binding; complete loss of phospholipase C-like activity toward cardiolipin; dbSNP:rs587777651
- C91 (= C84) binding
- R130 (= R121) to C: in HSD10MD; decreased stability; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization; complete loss of phospholipase C-like activity toward cardiolipin; dbSNP:rs28935475
- S155 (= S146) binding
- Q165 (= Q156) to H: in HSD10MD; loss of 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; does not bind NAD(+); complete loss of phospholipase C-like activity toward cardiolipin
- Y168 (= Y159) active site, Proton acceptor; binding
- K172 (= K163) binding ; mutation to A: Abolishes dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. Does not affect homotetramerization.
- V176 (≠ T167) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (= F192) binding
- T203 (= T194) binding
- P210 (≠ G201) to S: in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization
- K212 (≠ E203) to E: in HSD10MD; 4-fold decrease of 3-hydroxyacyl-CoA dehydrogenase activity; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing; dbSNP:rs886041974
- R226 (= R217) to Q: in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization; dbSNP:rs1556894502
- N247 (= N238) to S: in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization; dbSNP:rs122461163
- E249 (≠ T240) to Q: in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs62626305
Sites not aligning to the query:
- 12 V → L: in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
51% identity, 96% coverage: 9:250/251 of query aligns to 8:253/255 of 1u7tA
- active site: G15 (= G16), N115 (= N112), T147 (= T144), S149 (= S146), Y162 (= Y159), K166 (= K163), F195 (= F192)
- binding 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)ethanone adduct: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (≠ R37), D58 (= D57), V59 (= V58), C85 (= C84), A86 (= A85), G87 (= G86), A89 (= A88), V90 (≠ T89), A91 (≠ S90), T147 (= T144), S149 (= S146), Q156 (= Q153), Q159 (= Q156), Y162 (= Y159), K166 (= K163), P192 (= P189), L194 (≠ I191), F195 (= F192), T197 (= T194), L199 (≠ M196), L200 (= L197), L203 (= L200)
O08756 3-hydroxyacyl-CoA dehydrogenase type-2; 17-beta-estradiol 17-dehydrogenase; 2-methyl-3-hydroxybutyryl-CoA dehydrogenase; MHBD; 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)); 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase type II; 3alpha(or 20beta)-hydroxysteroid dehydrogenase; 7-alpha-hydroxysteroid dehydrogenase; Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Short chain dehydrogenase/reductase family 5C member 1; Short-chain type dehydrogenase/reductase XH98G2; Type II HADH; EC 1.1.1.35; EC 1.1.1.62; EC 1.1.1.239; EC 1.1.1.178; EC 1.1.1.53; EC 1.1.1.159 from Mus musculus (Mouse)
51% identity, 96% coverage: 9:250/251 of query aligns to 14:259/261 of O08756
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
O70351 3-hydroxyacyl-CoA dehydrogenase type-2; 17-beta-estradiol 17-dehydrogenase; 2-methyl-3-hydroxybutyryl-CoA dehydrogenase; MHBD; 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)); 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase type II; 3alpha(or 20beta)-hydroxysteroid dehydrogenase; 7-alpha-hydroxysteroid dehydrogenase; Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Short chain dehydrogenase/reductase family 5C member 1; Short-chain type dehydrogenase/reductase XH98G2; Type II HADH; EC 1.1.1.35; EC 1.1.1.62; EC 1.1.1.239; EC 1.1.1.178; EC 1.1.1.53; EC 1.1.1.159 from Rattus norvegicus (Rat) (see paper)
50% identity, 96% coverage: 9:250/251 of query aligns to 14:259/261 of O70351
- S155 (= S146) binding
- Y168 (= Y159) active site, Proton acceptor
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
50% identity, 96% coverage: 9:250/251 of query aligns to 8:253/255 of 1e3wD
- active site: G15 (= G16), N115 (= N112), T147 (= T144), S149 (= S146), Y162 (= Y159), K166 (= K163), F195 (= F192)
- binding acetoacetic acid: Y162 (= Y159), T202 (≠ G199)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ R37), N58 (≠ D57), V59 (= V58), C85 (= C84), A86 (= A85), G87 (= G86), V114 (≠ I111), T147 (= T144), Y162 (= Y159), K166 (= K163), P192 (= P189), L194 (≠ I191), F195 (= F192), T197 (= T194), L199 (≠ M196)
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
49% identity, 96% coverage: 9:250/251 of query aligns to 8:246/248 of 1e6wC
- active site: G15 (= G16), N115 (= N112), T147 (= T144), S149 (= S146), Y162 (= Y159), K166 (= K163), F195 (= F192)
- binding estradiol: Q159 (= Q156), Y162 (= Y159), L200 (= L197)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ R37), N58 (≠ D57), V59 (= V58), C85 (= C84), A86 (= A85), T147 (= T144), Y162 (= Y159), K166 (= K163), P192 (= P189), L194 (≠ I191), F195 (= F192), T197 (= T194), L199 (≠ M196)
2o23B The structure of wild-type human hadh2 (17beta-hydroxysteroid dehydrogenase type 10) bound to NAD+ at 1.2 a
50% identity, 96% coverage: 9:250/251 of query aligns to 14:251/255 of 2o23B
- active site: G21 (= G16), N121 (= N112), T153 (= T144), S155 (= S146), Y168 (= Y159), K172 (= K163), F201 (= F192)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), S20 (= S15), G21 (= G16), L22 (= L17), D41 (= D36), L42 (≠ R37), D64 (= D57), V65 (= V58), C91 (= C84), A92 (= A85), T153 (= T144), Y168 (= Y159), K172 (= K163), P198 (= P189), L200 (≠ I191), F201 (= F192), T203 (= T194), L205 (≠ M196)
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
54% identity, 98% coverage: 5:250/251 of query aligns to 1:238/241 of 1uayA
- active site: G12 (= G16), S134 (= S146), Y147 (= Y159), K151 (= K163)
- binding adenosine: G8 (= G12), S11 (= S15), D32 (= D36), L33 (≠ R37), D46 (= D57), V47 (= V58), A73 (= A85), G74 (= G86)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
48% identity, 99% coverage: 2:250/251 of query aligns to 4:255/258 of 3ppiA
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
46% identity, 97% coverage: 9:251/251 of query aligns to 12:258/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (≠ R37), S62 (≠ D57), V63 (= V58), C89 (= C84), A90 (= A85), S153 (= S146), Y166 (= Y159), K170 (= K163), P196 (= P189), G197 (= G190), I198 (= I191), F199 (= F192), T201 (= T194), M203 (= M196)
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
48% identity, 100% coverage: 1:250/251 of query aligns to 2:243/246 of 6ujkA
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), S16 (= S15), G17 (= G16), L18 (= L17), D37 (= D36), L38 (≠ T40), D57 (= D57), V58 (= V58), C83 (= C84), A84 (= A85), T142 (= T144), S144 (= S146), Y157 (= Y159), K161 (= K163), G188 (= G190), F190 (= F192), T192 (= T194), L194 (≠ M196)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
32% identity, 99% coverage: 2:250/251 of query aligns to 4:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N112), S139 (= S146), Q149 (= Q156), Y152 (= Y159), K156 (= K163)
- binding acetoacetyl-coenzyme a: D93 (≠ A91), K98 (≠ R96), S139 (= S146), N146 (≠ Q153), V147 (≠ K154), Q149 (= Q156), Y152 (= Y159), F184 (≠ I191), M189 (= M196), K200 (≠ A207)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ R37), V59 (≠ T56), D60 (= D57), V61 (= V58), N87 (≠ C84), A88 (= A85), G89 (= G86), I90 (≠ V87), T137 (= T144), S139 (= S146), Y152 (= Y159), K156 (= K163), P182 (= P189), F184 (≠ I191), T185 (≠ F192), T187 (= T194), M189 (= M196)
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
33% identity, 96% coverage: 9:250/251 of query aligns to 10:248/248 of 4cqmA
- active site: G17 (= G16), S143 (= S146), Y156 (= Y159), K160 (= K163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), S16 (= S15), G17 (= G16), I18 (≠ L17), D37 (= D36), L38 (≠ R37), A61 (≠ T56), V63 (= V58), C90 (= C84), A91 (= A85), G92 (= G86), I93 (≠ V87), V113 (≠ I111), I141 (≠ T144), S143 (= S146), Y156 (= Y159), K160 (= K163), P186 (= P189), G187 (= G190), I189 (≠ F192), T191 (= T194), P192 (= P195), M193 (= M196), T194 (≠ L197)
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
33% identity, 96% coverage: 9:250/251 of query aligns to 12:251/251 of 4cqlI
- active site: G19 (= G16), S146 (= S146), Y159 (= Y159), K163 (= K163)
- binding nicotinamide-adenine-dinucleotide: S18 (= S15), G19 (= G16), I20 (≠ L17), D39 (= D36), L40 (≠ R37), A64 (≠ T56), D65 (= D57), V66 (= V58), C93 (= C84), A94 (= A85), G95 (= G86), I96 (≠ V87), V116 (≠ I111), I144 (≠ T144), S146 (= S146), Y159 (= Y159), K163 (= K163), P189 (= P189), G190 (= G190), I192 (≠ F192), T194 (= T194), M196 (= M196)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
33% identity, 96% coverage: 9:250/251 of query aligns to 9:239/239 of 4nbtA
- active site: G16 (= G16), S132 (= S146), Y145 (= Y159), K149 (= K163)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ S15), G16 (= G16), L17 (= L17), D36 (= D36), L37 (≠ R37), L52 (≠ F54), N53 (≠ D57), V54 (= V58), N80 (≠ C84), A81 (= A85), G82 (= G86), I130 (≠ T144), S132 (= S146), Y145 (= Y159), K149 (= K163), P177 (= P189), G178 (= G190), I180 (≠ F192), T182 (= T194)
Q92506 (3R)-3-hydroxyacyl-CoA dehydrogenase; 17-beta-hydroxysteroid dehydrogenase 8; 17-beta-HSD 8; HSD17B8; 3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit; KAR alpha subunit; 3-oxoacyl-[acyl-carrier-protein] reductase; Estradiol 17-beta-dehydrogenase 8; Protein Ke6; Ke6; Short chain dehydrogenase/reductase family 30C member 1; Testosterone 17-beta-dehydrogenase 8; EC 1.1.1.n12; EC 1.1.1.62; EC 1.1.1.239 from Homo sapiens (Human) (see 2 papers)
32% identity, 96% coverage: 9:250/251 of query aligns to 15:261/261 of Q92506
- 15:23 (vs. 9:17, 67% identical) binding
- D42 (= D36) mutation to A: Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- DL 42:43 (≠ DR 36:37) binding
- ADV 74:76 (≠ TDV 56:58) binding
- R148 (= R138) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- V158 (≠ A148) to L: in a breast cancer sample; somatic mutation
- Y169 (= Y159) mutation to A: Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- YAASK 169:173 (= YAASK 159:163) binding
- K173 (= K163) mutation to A: Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- R189 (= R179) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- IAT 202:204 (≠ FRT 192:194) binding
Query Sequence
>3608297 Dshi_1700 short-chain dehydrogenase/reductase SDR (RefSeq)
MQVSDHAILVTGGASGLGEATVRHLRAKGAAVAVLDRDATRGHQLAAESGALFFETDVTD
DVSAEASVTAAATALGRITACVTCAGVATSAKTLGREGPHGLDAFQRTIDINLVGTFNIA
RLAAAEMARNAPDADGARGVIVTTASIAAFDGQKGQAAYAASKAGVTGLSLPMARDLARE
GIRVMSIAPGIFRTPMLIGLGEEIMEALAADVTFPKRLGDPVEYARLVAFILECGYLNGT
TIRLDGALRMP
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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