SitesBLAST
Comparing RR42_RS25375 FitnessBrowser__Cup4G11:RR42_RS25375 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)
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
61% identity, 100% coverage: 1:252/252 of query aligns to 4:255/255 of 4xgnA
- active site: Y161 (= Y158), K165 (= K162)
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (≠ R37), C59 (≠ T56), D60 (= D57), V61 (= V58), C86 (= C83), A87 (= A84), V113 (≠ I110), T146 (= T143), Y161 (= Y158), K165 (= K162), P191 (= P188), I193 (= I190), F194 (≠ M191), T196 (= T193), M198 (= M195)
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
60% identity, 100% coverage: 1:252/252 of query aligns to 7:261/261 of 4o5oB
Sites not aligning to the query:
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 3 papers)
51% identity, 98% coverage: 3:249/252 of query aligns to 2:253/255 of O18404
- L33 (≠ I34) mutation to Q: Lethal allele.
- F120 (= F116) mutation to I: Lethal allele.
- Q159 (= Q155) mutation Missing: Pupal lethal; pupation is developmentally delayed and pupae fail to enclose into adults. Larvae also display reduced levels of ATP, abnormal neuroblast mitochondrial morphology, and the accumulation of unprocessed mitochondrial tRNAs transcripts for tRNA(Ile), tRNA(Gly), tRNA(Val) and tRNA(Leu) (CUN).
- S163 (≠ A159) mutation to F: Pupal lethal; pupation is developmentally delayed and pupae fail to enclose into adults. Larvae also display reduced levels of ATP, abnormal neuroblast mitochondrial morphology, and the accumulation of unprocessed mitochondrial tRNAs transcripts for tRNA(Ile), tRNA(Gly), tRNA(Val) and tRNA(Leu) (CUN).
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
51% identity, 100% coverage: 1:252/252 of query aligns to 2:246/246 of 6ujkA
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), S16 (= S15), G17 (= G16), L18 (= L17), D37 (= D36), L38 (≠ R37), D57 (= D57), V58 (= V58), C83 (= C83), A84 (= A84), T142 (= T143), S144 (= S145), Y157 (= Y158), K161 (= K162), G188 (= G189), F190 (≠ M191), T192 (= T193), L194 (≠ M195)
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
52% identity, 96% coverage: 7:249/252 of query aligns to 6:253/255 of 1u7tA
- active site: G15 (= G16), N115 (= N111), T147 (= T143), S149 (= S145), Y162 (= Y158), K166 (= K162), F195 (≠ M191)
- 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 (= C83), A86 (= A84), G87 (= G85), A89 (= A87), V90 (≠ P88), A91 (= A89), T147 (= T143), S149 (= S145), Q156 (= Q152), Q159 (= Q155), Y162 (= Y158), K166 (= K162), P192 (= P188), L194 (≠ I190), F195 (≠ M191), T197 (= T193), L199 (≠ M195), L200 (= L196), L203 (≠ M199)
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)
52% identity, 96% coverage: 7:249/252 of query aligns to 12:259/261 of Q99714
- V12 (= V7) to L: in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing
- 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 (≠ R78) 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 (= C83) binding
- R130 (= R120) 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 (= S145) binding
- Q165 (= Q155) 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 (= Y158) active site, Proton acceptor; binding
- K172 (= K162) 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 (= V166) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (≠ M191) binding
- T203 (= T193) binding
- P210 (= P200) to S: in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization
- K212 (≠ E202) 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 (= R216) 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 (= N237) 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 (= E239) to Q: in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs62626305
8cbkC Structure of human mitochondrial rnase p in complex with mitochondrial pre-tRNA-his(5,ser) (see paper)
52% identity, 96% coverage: 7:249/252 of query aligns to 6:253/255 of 8cbkC
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (≠ R37), D58 (= D57), V59 (= V58), C85 (= C83), A86 (= A84), G87 (= G85), T147 (= T143), S149 (= S145), Y162 (= Y158), P192 (= P188), G193 (= G189), T197 (= T193), L199 (≠ M195)
- binding : S92 (≠ E90), K93 (= K91)
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: 7:249/252 of query aligns to 12:259/261 of O70351
- S155 (= S145) binding
- Y168 (= Y158) 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: 7:249/252 of query aligns to 6:253/255 of 1e3wD
- active site: G15 (= G16), N115 (= N111), T147 (= T143), S149 (= S145), Y162 (= Y158), K166 (= K162), F195 (≠ M191)
- binding acetoacetic acid: Y162 (= Y158), T202 (≠ G198)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ R37), N58 (≠ D57), V59 (= V58), C85 (= C83), A86 (= A84), G87 (= G85), V114 (≠ I110), T147 (= T143), Y162 (= Y158), K166 (= K162), P192 (= P188), L194 (≠ I190), F195 (≠ M191), T197 (= T193), L199 (≠ M195)
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
52% identity, 97% coverage: 9:252/252 of query aligns to 5:241/241 of 1uayA
- active site: G12 (= G16), S134 (= S145), Y147 (= Y158), K151 (= K162)
- binding adenosine: G8 (= G12), S11 (= S15), D32 (= D36), L33 (≠ R37), D46 (= D57), V47 (= V58), A73 (= A84), G74 (= G85)
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)
49% identity, 96% coverage: 7:249/252 of query aligns to 12:259/261 of O08756
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
49% identity, 96% coverage: 7:249/252 of query aligns to 6:246/248 of 1e6wC
- active site: G15 (= G16), N115 (= N111), T147 (= T143), S149 (= S145), Y162 (= Y158), K166 (= K162), F195 (≠ M191)
- binding estradiol: Q159 (= Q155), Y162 (= Y158), L200 (= L196)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ R37), N58 (≠ D57), V59 (= V58), C85 (= C83), A86 (= A84), T147 (= T143), Y162 (= Y158), K166 (= K162), P192 (= P188), L194 (≠ I190), F195 (≠ M191), T197 (= T193), L199 (≠ M195)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
50% identity, 97% coverage: 7:251/252 of query aligns to 10:259/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (≠ R37), S62 (≠ D57), V63 (= V58), C89 (= C83), A90 (= A84), S153 (= S145), Y166 (= Y158), K170 (= K162), P196 (= P188), G197 (= G189), I198 (= I190), F199 (≠ M191), T201 (= T193), M203 (= M195)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
44% identity, 100% coverage: 2:252/252 of query aligns to 4:258/258 of 3ppiA
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 98% coverage: 2:249/252 of query aligns to 4:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N111), S139 (= S145), Q149 (= Q155), Y152 (= Y158), K156 (= K162)
- binding acetoacetyl-coenzyme a: D93 (≠ E90), K98 (= K95), S139 (= S145), N146 (≠ Q152), V147 (= V153), Q149 (= Q155), Y152 (= Y158), F184 (≠ I190), M189 (= M195), K200 (≠ A206)
- 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 (≠ C83), A88 (= A84), G89 (= G85), I90 (≠ V86), T137 (= T143), S139 (= S145), Y152 (= Y158), K156 (= K162), P182 (= P188), F184 (≠ I190), T185 (≠ M191), T187 (= T193), M189 (= M195)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
35% identity, 97% coverage: 3:246/252 of query aligns to 6:237/240 of P73826
- S134 (= S145) mutation to A: 12% enzymatic activity.
- Y147 (= Y158) mutation to A: No enzymatic activity.
- K151 (= K162) mutation to A: 5% enzymatic activity.
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
32% identity, 96% coverage: 9:249/252 of query aligns to 12:251/251 of 4cqlI
- active site: G19 (= G16), S146 (= S145), Y159 (= Y158), K163 (= K162)
- binding nicotinamide-adenine-dinucleotide: S18 (= S15), G19 (= G16), I20 (≠ L17), D39 (= D36), L40 (≠ R37), A64 (≠ T56), D65 (= D57), V66 (= V58), C93 (= C83), A94 (= A84), G95 (= G85), I96 (≠ V86), V116 (≠ I110), I144 (≠ T143), S146 (= S145), Y159 (= Y158), K163 (= K162), P189 (= P188), G190 (= G189), I192 (≠ M191), T194 (= T193), M196 (= M195)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
32% identity, 97% coverage: 1:245/252 of query aligns to 4:243/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (≠ S15), G19 (= G16), I20 (≠ L17), D39 (= D36), R40 (= R37), C63 (≠ T56), I65 (≠ V58), N91 (≠ C83), G93 (= G85), I94 (≠ V86), V114 (≠ I110), Y155 (= Y158), K159 (= K162), I188 (≠ M191), T190 (= T193), T193 (≠ L196)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
32% identity, 97% coverage: 1:245/252 of query aligns to 3:250/255 of 5itvA
- active site: G18 (= G16), S141 (= S145), Y154 (= Y158), K158 (= K162)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (= S15), G18 (= G16), I19 (≠ L17), D38 (= D36), I39 (≠ R37), T61 (= T56), I63 (≠ V58), N89 (≠ C83), G91 (= G85), T139 (= T143), S141 (= S145), Y154 (= Y158), K158 (= K162), P184 (= P188), G185 (= G189), I186 (= I190), I187 (≠ M191)
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)
30% identity, 98% coverage: 2:249/252 of query aligns to 8:261/261 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 (= R137) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- V158 (≠ A147) to L: in a breast cancer sample; somatic mutation
- Y169 (= Y158) 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 158:162) binding
- K173 (= K162) 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 (= R178) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- IAT 202:204 (≠ MET 191:193) binding
Query Sequence
>RR42_RS25375 FitnessBrowser__Cup4G11:RR42_RS25375
MQIQDNVFIVTGGGSGLGAATVHALAENGAKVVIADRDADAGQAVAKTSGGAFVRTDVTD
EESVQGMYAFATRLGVLRGVINCAGVAPAEKVIGKSGVHAMASFSRTMQINVGGTFNVLR
LGAEIMAGQEALADGERGVIVNTASIAAFDGQVGQTAYAASKGAIVAMTLPLARELARFG
IRVMAIAPGIMETPMLLGMPAEVQKALGDAVPFPQRMGRPTEFADLVKHIIGSPYLNGEV
IRLDGAIRMAAK
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