SitesBLAST
Comparing WP_011906695.1 NCBI__GCF_000013325.1:WP_011906695.1 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)
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
55% identity, 99% coverage: 2:254/255 of query aligns to 1:255/255 of 1u7tA
- active site: G15 (= G16), N115 (= N113), T147 (= T146), S149 (= S148), Y162 (= Y161), K166 (= K165), F195 (= F194)
- 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 (= L37), D58 (≠ N57), V59 (= V58), C85 (= C84), A86 (= A85), G87 (= G86), A89 (≠ G88), V90 (≠ P89), A91 (≠ P90), T147 (= T146), S149 (= S148), Q156 (= Q155), Q159 (= Q158), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ I193), F195 (= F194), T197 (= T196), L199 (= L198), L200 (= L199), L203 (= L202)
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)
55% identity, 99% coverage: 2:254/255 of query aligns to 7:261/261 of Q99714
- V12 (≠ A7) to L: in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing
- S20 (= S15) binding NAD(+); mutation to F: Decreased dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation.
- L22 (= L17) binding NAD(+)
- D41 (= D36) binding NAD(+)
- D64 (≠ N57) binding NAD(+)
- V65 (= V58) binding NAD(+); to A: in HSD10MD; uncertain significance; dbSNP:rs104886492
- D86 (≠ R79) 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 NAD(+)
- R130 (≠ S122) 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 (= S148) binding substrate
- Q165 (= Q158) 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 (= Y161) active site, Proton acceptor; binding NAD(+)
- K172 (= K165) binding NAD(+); mutation to A: Abolishes dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. Does not affect homotetramerization.
- V176 (= V169) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (= F194) binding NAD(+)
- T203 (= T196) binding NAD(+)
- P210 (= P203) to S: in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization
- K212 (≠ E205) 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 (= R219) 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 (= N240) 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 (= E242) 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)
55% identity, 99% coverage: 2:254/255 of query aligns to 1:255/255 of 8cbkC
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (= L37), D58 (≠ N57), V59 (= V58), C85 (= C84), A86 (= A85), G87 (= G86), T147 (= T146), S149 (= S148), Y162 (= Y161), P192 (= P191), G193 (= G192), T197 (= T196), L199 (= L198)
- binding : S92 (≠ A91), K93 (= K92)
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
59% identity, 100% coverage: 1:255/255 of query aligns to 4:255/255 of 4xgnA
- active site: Y161 (= Y161), K165 (= K165)
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (= L37), C59 (≠ V56), D60 (≠ N57), V61 (= V58), C86 (= C84), A87 (= A85), V113 (≠ I112), T146 (= T146), Y161 (= Y161), K165 (= K165), P191 (= P191), I193 (= I193), F194 (= F194), T196 (= T196), M198 (≠ L198)
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)
53% identity, 99% coverage: 2:254/255 of query aligns to 7:261/261 of O70351
- S155 (= S148) binding substrate
- Y168 (= Y161) active site, Proton acceptor
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
53% identity, 99% coverage: 2:254/255 of query aligns to 1:255/255 of 1e3wD
- active site: G15 (= G16), N115 (= N113), T147 (= T146), S149 (= S148), Y162 (= Y161), K166 (= K165), F195 (= F194)
- binding acetoacetic acid: Y162 (= Y161), T202 (≠ S201)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ L37), N58 (= N57), V59 (= V58), C85 (= C84), A86 (= A85), G87 (= G86), V114 (≠ I112), T147 (= T146), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ I193), F195 (= F194), T197 (= T196), L199 (= L198)
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
57% identity, 100% coverage: 1:255/255 of query aligns to 2:246/246 of 6ujkA
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), S16 (= S15), G17 (= G16), L18 (= L17), D37 (= D36), L38 (= L37), D57 (≠ N57), V58 (= V58), C83 (= C84), A84 (= A85), T142 (= T146), S144 (= S148), Y157 (= Y161), K161 (= K165), G188 (= G192), F190 (= F194), T192 (= T196), L194 (= L198)
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)
53% identity, 99% coverage: 3:254/255 of query aligns to 2:255/255 of O18404
- L33 (= L34) mutation to Q: Lethal allele.
- F120 (= F118) mutation to I: Lethal allele.
- Q159 (= Q158) 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 (≠ A162) 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).
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)
52% identity, 99% coverage: 2:254/255 of query aligns to 7:261/261 of O08756
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
55% identity, 100% coverage: 1:255/255 of query aligns to 7:261/261 of 4o5oB
Sites not aligning to the query:
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
52% identity, 99% coverage: 2:254/255 of query aligns to 1:248/248 of 1e6wC
- active site: G15 (= G16), N115 (= N113), T147 (= T146), S149 (= S148), Y162 (= Y161), K166 (= K165), F195 (= F194)
- binding estradiol: Q159 (= Q158), Y162 (= Y161), L200 (= L199)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ L37), N58 (= N57), V59 (= V58), C85 (= C84), A86 (= A85), T147 (= T146), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ I193), F195 (= F194), T197 (= T196), L199 (= L198)
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
53% identity, 98% coverage: 7:255/255 of query aligns to 3:241/241 of 1uayA
- active site: G12 (= G16), S134 (= S148), Y147 (= Y161), K151 (= K165)
- binding adenosine: G8 (= G12), S11 (= S15), D32 (= D36), L33 (= L37), D46 (≠ N57), V47 (= V58), A73 (= A85), G74 (= G86)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
47% identity, 98% coverage: 4:252/255 of query aligns to 7:257/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (= L37), S62 (≠ N57), V63 (= V58), C89 (= C84), A90 (= A85), S153 (= S148), Y166 (= Y161), K170 (= K165), P196 (= P191), G197 (= G192), I198 (= I193), F199 (= F194), T201 (= T196), M203 (≠ L198)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
46% identity, 100% coverage: 2:255/255 of query aligns to 4:258/258 of 3ppiA
4nbuB Crystal structure of fabg from bacillus sp (see paper)
35% identity, 98% coverage: 3:252/255 of query aligns to 5:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N113), S139 (= S148), Q149 (= Q158), Y152 (= Y161), K156 (= K165)
- binding acetoacetyl-coenzyme a: D93 (= D97), K98 (≠ P100), S139 (= S148), N146 (≠ Q155), V147 (≠ I156), Q149 (= Q158), Y152 (= Y161), F184 (≠ I193), M189 (≠ L198), K200 (≠ S209)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ L37), V59 (= V56), D60 (≠ N57), V61 (= V58), N87 (≠ C84), A88 (= A85), G89 (= G86), I90 (= I87), T137 (= T146), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), F184 (≠ I193), T185 (≠ F194), T187 (= T196), M189 (≠ L198)
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
34% identity, 95% coverage: 10:252/255 of query aligns to 11:239/241 of 4cqmF
- active site: G17 (= G16), S139 (= S148), Q149 (= Q158), Y152 (= Y161), K156 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), R16 (≠ S15), G17 (= G16), I18 (≠ L17), A37 (≠ D36), R38 (≠ L37), N39 (= N38), D60 (≠ N57), V61 (= V58), A87 (≠ C84), A88 (= A85), G89 (= G86), V137 (≠ T146), S139 (= S148), Y152 (= Y161), K156 (= K165), V185 (≠ F194), T187 (= T196), M189 (≠ L198)
Q8N4T8 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-[acyl-carrier-protein] reductase beta subunit; KAR beta subunit; Carbonyl reductase family member 4; CBR4; Quinone reductase CBR4; Short chain dehydrogenase/reductase family 45C member 1; EC 1.1.1.100; EC 1.6.5.10 from Homo sapiens (Human) (see 4 papers)
34% identity, 95% coverage: 10:252/255 of query aligns to 7:235/237 of Q8N4T8
- G9 (= G12) mutation to S: Unable to restore growth of an OAR1-deficient yeast mutant.
- SRGI 11:14 (≠ ASGL 14:17) binding NADP(+)
- R12 (≠ S15) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
- R34 (≠ L37) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- RN 34:35 (≠ LN 37:38) binding NADP(+)
- D56 (≠ N57) binding NADP(+)
- L70 (≠ A71) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ CAG 84:86) binding NADP(+)
- S135 (= S148) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y161) binding NADP(+); mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K165) binding NADP(+); mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- R168 (= R181) mutation to E: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- K169 (≠ Y182) mutation to E: Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- VHT 181:183 (≠ FWT 194:196) binding NADP(+)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
34% identity, 95% coverage: 9:249/255 of query aligns to 12:237/240 of P73826
- S134 (= S148) mutation to A: 12% enzymatic activity.
- Y147 (= Y161) mutation to A: No enzymatic activity.
- K151 (= K165) mutation to A: 5% enzymatic activity.
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
34% identity, 98% coverage: 3:252/255 of query aligns to 3:239/239 of 4nbtA
- active site: G16 (= G16), S132 (= S148), Y145 (= Y161), K149 (= K165)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ S15), G16 (= G16), L17 (= L17), D36 (= D40), L37 (= L41), L52 (≠ V56), N53 (= N57), V54 (= V58), N80 (≠ C84), A81 (= A85), G82 (= G86), I130 (≠ T146), S132 (= S148), Y145 (= Y161), K149 (= K165), P177 (= P191), G178 (= G192), I180 (≠ F194), T182 (= T196)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
35% identity, 98% coverage: 3:253/255 of query aligns to 8:253/258 of 4wecA
- active site: G21 (= G16), S143 (= S148), Q154 (= Q158), Y157 (= Y161), K161 (= K165)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), A19 (= A14), S20 (= S15), G21 (= G16), I22 (≠ L17), D41 (= D36), I42 (≠ L37), V61 (= V56), D62 (≠ N57), V63 (= V58), N89 (≠ C84), T141 (= T146), Y157 (= Y161), K161 (= K165), P187 (= P191), P189 (≠ I193), V190 (≠ F194)
Query Sequence
>WP_011906695.1 NCBI__GCF_000013325.1:WP_011906695.1
MDIQGLAAIVTGGASGLGAATAELLAARGAKVTLFDLNADLGNAKAAEIGGRFAAVNVTD
EDAVANAIAEAEAVNGKARILVNCAGIGPPAKVLNRDGSPLPLADFARIININLLGTFNV
LSKFASRIHDAEPLNEDGERGVIVNTASVAAFEGQIGQPAYAASKGGVVGMALPIAREFA
RYGIRVNTIAPGIFWTRLLGSLPQEAQDSLGRQVPFPSRLGKPAEYAKMVEAIVTNPMLN
AEVIRLDGAIRMAPK
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