SitesBLAST
Comparing WP_004321104.1 NCBI__GCF_000310185.1:WP_004321104.1 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)
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
69% 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 (≠ T58), D60 (= D59), V61 (= V60), C86 (= C86), A87 (= A87), V113 (≠ I113), T146 (= T146), Y161 (= Y161), K165 (= K165), P191 (= P191), I193 (= I193), F194 (= F194), T196 (= T196), M198 (= M198)
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
65% identity, 100% coverage: 1:255/255 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)
57% identity, 98% coverage: 3:252/255 of query aligns to 2:253/255 of O18404
- L33 (= L34) mutation to Q: Lethal allele.
- F120 (= F119) 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).
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
55% identity, 96% coverage: 7:252/255 of query aligns to 6:253/255 of 1u7tA
- active site: G15 (= G16), N115 (= N114), 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 (= D59), V59 (= V60), C85 (= C86), A86 (= A87), G87 (= G88), A89 (= A90), V90 (≠ P91), A91 (≠ G92), T147 (= T146), S149 (= S148), Q156 (= Q155), Q159 (= Q158), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ I193), F195 (= F194), T197 (= T196), L199 (≠ M198), L200 (= L199), L203 (= L202)
8cbkC Structure of human mitochondrial rnase p in complex with mitochondrial pre-tRNA-his(5,ser) (see paper)
55% identity, 96% coverage: 7:252/255 of query aligns to 6:253/255 of 8cbkC
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (= L37), D58 (= D59), V59 (= V60), C85 (= C86), A86 (= A87), G87 (= G88), T147 (= T146), S149 (= S148), Y162 (= Y161), P192 (= P191), G193 (= G192), T197 (= T196), L199 (≠ M198)
- binding : S92 (≠ E93), K93 (= K94)
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, 96% coverage: 7:252/255 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 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 (= D59) binding NAD(+)
- V65 (= V60) binding NAD(+); to A: in HSD10MD; uncertain significance; dbSNP:rs104886492
- D86 (≠ H81) 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 (= C86) binding NAD(+)
- R130 (= R123) 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 (≠ A205) 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
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
57% identity, 97% coverage: 9:255/255 of query aligns to 5:241/241 of 1uayA
- active site: G12 (= G16), S134 (= S148), Y147 (= Y161), K151 (= K165)
- binding adenosine: G8 (= G12), S11 (= S15), D32 (= D36), L33 (= L37), D46 (= D59), V47 (= V60), A73 (= A87), G74 (= G88)
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, 96% coverage: 7:252/255 of query aligns to 12:259/261 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, 96% coverage: 7:252/255 of query aligns to 6:253/255 of 1e3wD
- active site: G15 (= G16), N115 (= N114), T147 (= T146), S149 (= S148), Y162 (= Y161), K166 (= K165), F195 (= F194)
- binding acetoacetic acid: Y162 (= Y161), T202 (≠ G201)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ L37), N58 (≠ D59), V59 (= V60), C85 (= C86), A86 (= A87), G87 (= G88), V114 (≠ I113), T147 (= T146), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ I193), F195 (= F194), T197 (= T196), L199 (≠ M198)
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)
53% identity, 96% coverage: 7:252/255 of query aligns to 12:259/261 of O08756
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
55% 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 (= D59), V58 (= V60), C83 (= C86), A84 (= A87), T142 (= T146), S144 (= S148), Y157 (= Y161), K161 (= K165), G188 (= G192), F190 (= F194), T192 (= T196), L194 (≠ M198)
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
52% identity, 96% coverage: 7:252/255 of query aligns to 6:246/248 of 1e6wC
- active site: G15 (= G16), N115 (= N114), 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 (≠ D59), V59 (= V60), C85 (= C86), A86 (= A87), T147 (= T146), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ I193), F195 (= F194), T197 (= T196), L199 (≠ M198)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
46% identity, 97% coverage: 7:254/255 of query aligns to 10:259/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (= L37), S62 (≠ D59), V63 (= V60), C89 (= C86), A90 (= A87), S153 (= S148), Y166 (= Y161), K170 (= K165), P196 (= P191), G197 (= G192), I198 (= I193), F199 (= F194), T201 (= T196), M203 (= M198)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
46% identity, 97% coverage: 9:255/255 of query aligns to 11:258/258 of 3ppiA
4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 98% coverage: 2:252/255 of query aligns to 4:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N114), S139 (= S148), Q149 (= Q158), Y152 (= Y161), K156 (= K165)
- binding acetoacetyl-coenzyme a: D93 (≠ G92), K98 (≠ P101), S139 (= S148), N146 (≠ Q155), V147 (≠ I156), Q149 (= Q158), Y152 (= Y161), F184 (≠ I193), M189 (= M198), K200 (≠ S209)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ L37), V59 (≠ T58), D60 (= D59), V61 (= V60), N87 (≠ C86), A88 (= A87), G89 (= G88), I90 (≠ V89), T137 (= T146), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), F184 (≠ I193), T185 (≠ F194), T187 (= T196), M189 (= M198)
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
39% identity, 88% coverage: 2:225/255 of query aligns to 3:207/244 of 1nfqA
- active site: G17 (= G16), S139 (= S148), Y152 (= Y161), K156 (= K165)
- binding Androsterone: L91 (≠ A90), E141 (≠ A150), C149 (≠ Q158), Y152 (= Y161), V193 (≠ L202), I197 (≠ V206), F198 (= F216)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (≠ S15), G17 (= G16), M18 (≠ L17), D37 (= D36), L39 (≠ N38), L59 (≠ T58), D60 (= D59), V61 (= V60), N87 (≠ C86), A88 (= A87), I137 (≠ T146), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), V185 (≠ F194), T187 (= T196), P188 (= P197), M189 (= M198), T190 (≠ L199)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
39% identity, 88% coverage: 2:225/255 of query aligns to 3:207/244 of 1nffA
- active site: G17 (= G16), S139 (= S148), Y152 (= Y161), K156 (= K165)
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), R16 (≠ S15), G17 (= G16), M18 (≠ L17), D37 (= D36), I38 (≠ L37), L39 (≠ N38), L59 (≠ T58), D60 (= D59), V61 (= V60), N87 (≠ C86), A88 (= A87), G89 (= G88), I90 (≠ V89), I137 (≠ T146), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), V185 (≠ F194), T187 (= T196), P188 (= P197), M189 (= M198), T190 (≠ L199)
P9WGT1 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase; NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase; EC 1.1.1.53 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
38% identity, 88% coverage: 2:225/255 of query aligns to 4:208/260 of P9WGT1
- I6 (≠ A4) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ SGL 15:17) binding NAD(+)
- D38 (= D36) binding NAD(+)
- V47 (≠ L45) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 59:60) binding NAD(+)
- T69 (≠ Q67) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (≠ C86) binding NAD(+)
- S140 (= S148) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y161) binding NAD(+); mutation to F: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- K157 (= K165) binding NAD(+)
- 183:191 (vs. 191:199, 56% identical) binding NAD(+)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
32% identity, 97% coverage: 3:249/255 of query aligns to 6:237/240 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.
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
32% identity, 99% coverage: 1:253/255 of query aligns to 3:245/245 of 5t5qC
- active site: G18 (= G16), S140 (= S148), N150 (≠ Q158), Y153 (= Y161), K157 (= K165)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ A14), G17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), L39 (= L37), D63 (= D59), A64 (≠ V60), S90 (≠ C86), I113 (= I113), Y153 (= Y161), K157 (= K165), P182 (= P191), I185 (≠ F194), T187 (= T196), M189 (= M198)
Query Sequence
>WP_004321104.1 NCBI__GCF_000310185.1:WP_004321104.1
MKIANSVFLVTGGASGLGAATARMVVEGGGRVVLADLNEEAGKALAAELGAAARFVRTDV
TDEASTQAAVEAAVQGCGGLHGLVCCAGVAPGEKVVGKDGPHGLDRFVRGVMINLVGTFN
PIRLAAAAMSKAAPNEEGERGVIVTTASVAAFDGQIGQATYAASKAGVVGMTLPIARELA
RYGIRVMSIAPGIFETPMLRGLPQAVQDSLGEMVPFPSRLGRSSEYAQLVRSICENPMLN
GEVIRLDGAIRMAAK
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