SitesBLAST
Comparing RR42_RS36415 FitnessBrowser__Cup4G11:RR42_RS36415 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)
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, 97% coverage: 9:259/260 of query aligns to 7:255/255 of O18404
- L33 (= L35) mutation to Q: Lethal allele.
- F120 (= F125) mutation to I: Lethal allele.
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)
52% identity, 97% coverage: 7:259/260 of query aligns to 11:261/261 of O70351
- S155 (= S153) binding
- Y168 (= Y166) active site, Proton acceptor
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
52% identity, 97% coverage: 7:259/260 of query aligns to 5:255/255 of 1e3wD
- active site: G15 (= G17), N115 (= N120), T147 (= T151), S149 (= S153), Y162 (= Y166), K166 (= K170), F195 (= F199)
- binding acetoacetic acid: Y162 (= Y166), T202 (≠ G206)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), S14 (= S16), G15 (= G17), L16 (= L18), D35 (= D37), V36 (≠ M38), N58 (= N58), V59 (= V59), C85 (= C85), A86 (= A86), G87 (= G87), V114 (≠ I119), T147 (= T151), Y162 (= Y166), K166 (= K170), P192 (= P196), L194 (≠ I198), F195 (= F199), T197 (= T201), L199 (= L203)
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)
50% identity, 97% coverage: 7:259/260 of query aligns to 11:261/261 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)
51% identity, 97% coverage: 7:259/260 of query aligns to 5:248/248 of 1e6wC
- active site: G15 (= G17), N115 (= N120), T147 (= T151), S149 (= S153), Y162 (= Y166), K166 (= K170), F195 (= F199)
- binding estradiol: Q159 (= Q163), Y162 (= Y166), L200 (= L204)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), S14 (= S16), G15 (= G17), L16 (= L18), D35 (= D37), V36 (≠ M38), N58 (= N58), V59 (= V59), C85 (= C85), A86 (= A86), T147 (= T151), Y162 (= Y166), K166 (= K170), P192 (= P196), L194 (≠ I198), F195 (= F199), T197 (= T201), L199 (= L203)
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
53% identity, 100% coverage: 1:260/260 of query aligns to 4:255/255 of 4xgnA
- active site: Y161 (= Y166), K165 (= K170)
- binding nicotinamide-adenine-dinucleotide: G15 (= G13), S18 (= S16), G19 (= G17), L20 (= L18), D39 (= D37), L40 (≠ M38), C59 (≠ V57), D60 (≠ N58), V61 (= V59), C86 (= C85), A87 (= A86), V113 (≠ I119), T146 (= T151), Y161 (= Y166), K165 (= K170), P191 (= P196), I193 (= I198), F194 (= F199), T196 (= T201), M198 (≠ L203)
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
51% identity, 97% coverage: 7:259/260 of query aligns to 5:255/255 of 1u7tA
- active site: G15 (= G17), N115 (= N120), T147 (= T151), S149 (= S153), Y162 (= Y166), K166 (= K170), F195 (= F199)
- binding 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)ethanone adduct: G11 (= G13), S14 (= S16), G15 (= G17), L16 (= L18), D35 (= D37), L36 (≠ M38), D58 (≠ N58), V59 (= V59), C85 (= C85), A86 (= A86), G87 (= G87), A89 (≠ G89), V90 (≠ N90), A91 (= A91), T147 (= T151), S149 (= S153), Q156 (= Q160), Q159 (= Q163), Y162 (= Y166), K166 (= K170), P192 (= P196), L194 (≠ I198), F195 (= F199), T197 (= T201), L199 (= L203), L200 (= L204), L203 (≠ A207)
7onuC Structure of human mitochondrial rnase p in complex with mitochondrial pre-tRNA-tyr (see paper)
51% identity, 97% coverage: 7:259/260 of query aligns to 5:255/255 of 7onuC
- binding nicotinamide-adenine-dinucleotide: S14 (= S16), G15 (= G17), L16 (= L18), D35 (= D37), L36 (≠ M38), V59 (= V59), C85 (= C85), S149 (= S153), Y162 (= Y166), F195 (= F199), T197 (= T201)
- binding : S92 (≠ I92), K93 (= K93)
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, 97% coverage: 7:259/260 of query aligns to 11:261/261 of Q99714
- V12 (≠ T8) to L: in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing
- S20 (= S16) binding ; mutation to F: Decreased dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation.
- L22 (= L18) binding
- D41 (= D37) binding
- D64 (≠ N58) binding
- V65 (= V59) binding ; to A: in HSD10MD; uncertain significance; dbSNP:rs104886492
- D86 (≠ R80) 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 (= C85) binding
- R130 (= R130) 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 (= S153) binding
- Q165 (= Q163) 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 (= Y166) active site, Proton acceptor; binding
- K172 (= K170) 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 (= V174) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (= F199) binding
- T203 (= T201) binding
- P210 (≠ Q208) to S: in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization
- K212 (≠ H210) 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 (= R224) 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 (= N245) 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 (= E247) to Q: in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs62626305
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
51% identity, 97% coverage: 8:260/260 of query aligns to 8:246/246 of 6ujkA
- binding nicotinamide-adenine-dinucleotide: G13 (= G13), S16 (= S16), G17 (= G17), L18 (= L18), D37 (= D37), L38 (≠ M38), D57 (≠ N58), V58 (= V59), C83 (= C85), A84 (= A86), T142 (= T151), S144 (= S153), Y157 (= Y166), K161 (= K170), G188 (= G197), F190 (= F199), T192 (= T201), L194 (= L203)
2o23B The structure of wild-type human hadh2 (17beta-hydroxysteroid dehydrogenase type 10) bound to NAD+ at 1.2 a
50% identity, 97% coverage: 7:259/260 of query aligns to 11:253/255 of 2o23B
- active site: G21 (= G17), N121 (= N120), T153 (= T151), S155 (= S153), Y168 (= Y166), K172 (= K170), F201 (= F199)
- binding nicotinamide-adenine-dinucleotide: G17 (= G13), S20 (= S16), G21 (= G17), L22 (= L18), D41 (= D37), L42 (≠ M38), D64 (≠ N58), V65 (= V59), C91 (= C85), A92 (= A86), T153 (= T151), Y168 (= Y166), K172 (= K170), P198 (= P196), L200 (≠ I198), F201 (= F199), T203 (= T201), L205 (= L203)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
44% identity, 97% coverage: 7:257/260 of query aligns to 9:257/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G13), S18 (= S16), G19 (= G17), L20 (= L18), D39 (= D37), L40 (≠ M38), S62 (≠ N58), V63 (= V59), C89 (= C85), A90 (= A86), S153 (= S153), Y166 (= Y166), K170 (= K170), P196 (= P196), G197 (= G197), I198 (= I198), F199 (= F199), T201 (= T201), M203 (≠ L203)
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
50% identity, 97% coverage: 8:260/260 of query aligns to 3:241/241 of 1uayA
- active site: G12 (= G17), S134 (= S153), Y147 (= Y166), K151 (= K170)
- binding adenosine: G8 (= G13), S11 (= S16), D32 (= D37), L33 (≠ M38), D46 (≠ N58), V47 (= V59), A73 (= A86), G74 (= G87)
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
49% identity, 97% coverage: 10:260/260 of query aligns to 15:261/261 of 4o5oB
Sites not aligning to the query:
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
44% identity, 97% coverage: 8:260/260 of query aligns to 9:258/258 of 3ppiA
4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 96% coverage: 9:257/260 of query aligns to 10:244/244 of 4nbuB
- active site: G18 (= G17), N111 (= N120), S139 (= S153), Q149 (= Q163), Y152 (= Y166), K156 (= K170)
- binding acetoacetyl-coenzyme a: D93 (≠ T94), K98 (= K99), S139 (= S153), N146 (≠ Q160), V147 (≠ M161), Q149 (= Q163), Y152 (= Y166), F184 (≠ I198), M189 (≠ L203), K200 (≠ A214)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ S16), G18 (= G17), I19 (≠ L18), D38 (= D37), F39 (≠ M38), V59 (= V57), D60 (≠ N58), V61 (= V59), N87 (≠ C85), A88 (= A86), G89 (= G87), I90 (≠ T88), T137 (= T151), S139 (= S153), Y152 (= Y166), K156 (= K170), P182 (= P196), F184 (≠ I198), T185 (≠ F199), T187 (= T201), M189 (≠ L203)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
38% identity, 97% coverage: 5:255/260 of query aligns to 7:245/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G13), R18 (≠ S16), G19 (= G17), I20 (≠ L18), D39 (= D37), R40 (≠ M38), C63 (≠ V57), I65 (≠ V59), N91 (≠ C85), G93 (= G87), I94 (≠ T88), V114 (≠ I119), Y155 (= Y166), K159 (= K170), I188 (≠ F199), T190 (= T201), T193 (≠ L204)
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
35% identity, 88% coverage: 10:238/260 of query aligns to 13:229/251 of 6d9yB
- active site: G20 (= G17), S145 (= S153), Y158 (= Y166)
- binding nicotinamide-adenine-dinucleotide: G16 (= G13), R19 (≠ S16), G20 (= G17), D40 (= D37), L41 (≠ M38), V64 (= V59), D65 (vs. gap), Q66 (vs. gap), A93 (= A86), S145 (= S153), Y158 (= Y166), K162 (= K170), P188 (= P196), A189 (≠ G197), A190 (≠ I198), A191 (≠ F199), T193 (= T201)
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
30% identity, 97% coverage: 6:257/260 of query aligns to 8:251/251 of 4cqlI
- active site: G19 (= G17), S146 (= S153), Y159 (= Y166), K163 (= K170)
- binding nicotinamide-adenine-dinucleotide: S18 (= S16), G19 (= G17), I20 (≠ L18), D39 (= D37), L40 (≠ M38), A64 (= A67), D65 (≠ G68), V66 (≠ F69), C93 (≠ S96), A94 (≠ R97), G95 (≠ A98), I96 (≠ K99), V116 (≠ I119), I144 (≠ T151), S146 (= S153), Y159 (= Y166), K163 (= K170), P189 (= P196), G190 (= G197), I192 (≠ F199), T194 (= T201), M196 (≠ L203)
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, 97% coverage: 6:257/260 of query aligns to 11:261/261 of Q92506
- 15:23 (vs. 10:18, 44% identical) binding
- D42 (= D37) 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 (≠ DM 37:38) binding
- ADV 74:76 (≠ AGF 67:69) binding
- R148 (= R145) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- V158 (≠ A155) to L: in a breast cancer sample; somatic mutation
- Y169 (= Y166) 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 (≠ YSASK 166:170) binding
- K173 (= K170) 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 (≠ G186) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- IAT 202:204 (≠ FNT 199:201) binding
Query Sequence
>RR42_RS36415 FitnessBrowser__Cup4G11:RR42_RS36415
MELNASVTAVITGGASGLGEATARALAAHGVRVALFDMNAEKGEAVARELGGVFCQVNVT
SEAEVEAGFAKARAALGQERILVNCAGTGNAIKTASRAKEAPDQIRFFASDAFERIIQIN
LIGSFRCLARSAAGMLTLDARDGDRGVIINTASVAAQDGQMGQAAYSASKAGVVGMTLPI
ARDLSGEGIRVNTIMPGIFNTPLLQGAQEHVKAALAASVPFPKRLGAPEEFASLALEMCR
NSYFNGEAVRLDGAIRMAPR
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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