SitesBLAST
Comparing RR42_RS03005 FitnessBrowser__Cup4G11:RR42_RS03005 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)
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
56% identity, 100% coverage: 1:254/254 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 (= C85), A84 (= A86), T142 (= T145), S144 (= S147), Y157 (= Y160), K161 (= K164), G188 (= G191), F190 (= F193), T192 (= T195), L194 (= L197)
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)
48% identity, 99% coverage: 3:253/254 of query aligns to 2:255/255 of O18404
- L33 (≠ I34) mutation to Q: Lethal allele.
- F120 (= F119) mutation to I: Lethal allele.
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
51% identity, 100% coverage: 1:254/254 of query aligns to 4:255/255 of 4xgnA
- active site: Y161 (= Y160), K165 (= K164)
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (= L37), C59 (≠ A58), D60 (= D59), V61 (= V60), C86 (= C85), A87 (= A86), V113 (≠ I113), T146 (= T145), Y161 (= Y160), K165 (= K164), P191 (= P190), I193 (≠ L192), F194 (= F193), T196 (= T195), M198 (≠ L197)
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
49% identity, 98% coverage: 6:253/254 of query aligns to 5:255/255 of 1u7tA
- active site: G15 (= G16), N115 (= N114), T147 (= T145), S149 (= S147), Y162 (= Y160), K166 (= K164), F195 (= F193)
- 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 (= C85), A86 (= A86), G87 (= G87), A89 (≠ G89), V90 (≠ G90), A91 (≠ P91), T147 (= T145), S149 (= S147), Q156 (= Q154), Q159 (= Q157), Y162 (= Y160), K166 (= K164), P192 (= P190), L194 (= L192), F195 (= F193), T197 (= T195), L199 (= L197), L200 (= L198), L203 (= L201)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
48% identity, 98% coverage: 7:254/254 of query aligns to 9:258/258 of 3ppiA
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)
47% identity, 98% coverage: 6:253/254 of query aligns to 11:261/261 of O70351
- S155 (= S147) binding
- Y168 (= Y160) active site, Proton acceptor
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
47% identity, 98% coverage: 6:253/254 of query aligns to 5:255/255 of 1e3wD
- active site: G15 (= G16), N115 (= N114), T147 (= T145), S149 (= S147), Y162 (= Y160), K166 (= K164), F195 (= F193)
- binding acetoacetic acid: Y162 (= Y160), T202 (≠ R200)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ L37), N58 (≠ D59), V59 (= V60), C85 (= C85), A86 (= A86), G87 (= G87), V114 (≠ I113), T147 (= T145), Y162 (= Y160), K166 (= K164), P192 (= P190), L194 (= L192), F195 (= F193), T197 (= T195), L199 (= L197)
7onuC Structure of human mitochondrial rnase p in complex with mitochondrial pre-tRNA-tyr (see paper)
49% identity, 98% coverage: 6:253/254 of query aligns to 5:255/255 of 7onuC
- binding nicotinamide-adenine-dinucleotide: S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (= L37), V59 (= V60), C85 (= C85), S149 (= S147), Y162 (= Y160), F195 (= F193), T197 (= T195)
- binding : S92 (≠ V92), K93 (≠ R93)
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)
49% identity, 98% coverage: 6:253/254 of query aligns to 11:261/261 of Q99714
- V12 (≠ S7) 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 (= D59) binding
- V65 (= V60) 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 (= 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 (= S147) binding
- Q165 (= Q157) 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 (= Y160) active site, Proton acceptor; binding
- K172 (= K164) 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 (= V168) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (= F193) binding
- T203 (= T195) binding
- P210 (= P202) to S: in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization
- K212 (≠ N204) 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 (= R218) 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 (= N239) 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 (= E241) to Q: in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs62626305
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)
47% identity, 98% coverage: 6:253/254 of query aligns to 11:261/261 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
48% identity, 100% coverage: 1:254/254 of query aligns to 7:261/261 of 4o5oB
Sites not aligning to the query:
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
52% identity, 98% coverage: 7:254/254 of query aligns to 3:241/241 of 1uayA
- active site: G12 (= G16), S134 (= S147), Y147 (= Y160), K151 (= K164)
- binding adenosine: G8 (= G12), S11 (= S15), D32 (= D36), L33 (= L37), D46 (= D59), V47 (= V60), A73 (= A86), G74 (= G87)
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
45% identity, 98% coverage: 6:253/254 of query aligns to 5:248/248 of 1e6wC
- active site: G15 (= G16), N115 (= N114), T147 (= T145), S149 (= S147), Y162 (= Y160), K166 (= K164), F195 (= F193)
- binding estradiol: Q159 (= Q157), Y162 (= Y160), L200 (= L198)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ L37), N58 (≠ D59), V59 (= V60), C85 (= C85), A86 (= A86), T147 (= T145), Y162 (= Y160), K166 (= K164), P192 (= P190), L194 (= L192), F195 (= F193), T197 (= T195), L199 (= L197)
2o23B The structure of wild-type human hadh2 (17beta-hydroxysteroid dehydrogenase type 10) bound to NAD+ at 1.2 a
48% identity, 98% coverage: 6:253/254 of query aligns to 11:253/255 of 2o23B
- active site: G21 (= G16), N121 (= N114), T153 (= T145), S155 (= S147), Y168 (= Y160), K172 (= K164), F201 (= F193)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), S20 (= S15), G21 (= G16), L22 (= L17), D41 (= D36), L42 (= L37), D64 (= D59), V65 (= V60), C91 (= C85), A92 (= A86), T153 (= T145), Y168 (= Y160), K172 (= K164), P198 (= P190), L200 (= L192), F201 (= F193), T203 (= T195), L205 (= L197)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
43% identity, 97% coverage: 6:251/254 of query aligns to 9:257/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (= L37), S62 (≠ D59), V63 (= V60), C89 (= C85), A90 (= A86), S153 (= S147), Y166 (= Y160), K170 (= K164), P196 (= P190), G197 (= G191), I198 (≠ L192), F199 (= F193), T201 (= T195), M203 (≠ L197)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
33% identity, 98% coverage: 2:251/254 of query aligns to 4:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N114), S139 (= S147), Q149 (= Q157), Y152 (= Y160), K156 (= K164)
- binding acetoacetyl-coenzyme a: D93 (≠ P91), K98 (≠ E96), S139 (= S147), N146 (≠ Q154), V147 (≠ I155), Q149 (= Q157), Y152 (= Y160), F184 (≠ L192), M189 (≠ L197), K200 (≠ S208)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ L37), V59 (≠ A58), D60 (= D59), V61 (= V60), N87 (≠ C85), A88 (= A86), G89 (= G87), I90 (≠ V88), T137 (= T145), S139 (= S147), Y152 (= Y160), K156 (= K164), P182 (= P190), F184 (≠ L192), T185 (≠ F193), T187 (= T195), M189 (≠ L197)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
33% identity, 98% coverage: 1:249/254 of query aligns to 4:245/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (≠ S15), G19 (= G16), I20 (≠ L17), D39 (= D36), R40 (≠ L37), C63 (≠ A58), I65 (≠ V60), N91 (≠ C85), G93 (= G87), I94 (≠ V88), V114 (≠ I113), Y155 (= Y160), K159 (= K164), I188 (≠ F193), T190 (= T195), T193 (≠ L198)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
36% identity, 93% coverage: 1:235/254 of query aligns to 1:227/248 of Q9KJF1
- M1 (= M1) modified: Initiator methionine, Removed
- S15 (= S15) binding
- D36 (= D36) binding
- D62 (= D62) binding
- I63 (≠ T63) binding
- N89 (≠ C85) binding
- Y153 (= Y160) binding
- K157 (= K164) binding
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
35% identity, 92% coverage: 3:235/254 of query aligns to 2:226/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), M16 (≠ L17), D35 (= D36), I36 (≠ L37), I62 (≠ T63), N88 (≠ C85), G90 (= G87), I138 (≠ T145), S140 (= S147), Y152 (= Y160), K156 (= K164), I185 (≠ F193)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
30% identity, 98% coverage: 2:251/254 of query aligns to 2:239/239 of 4nbtA
- active site: G16 (= G16), S132 (= S147), Y145 (= Y160), K149 (= K164)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ S15), G16 (= G16), L17 (= L17), D36 (= D36), L37 (= L37), L52 (= L52), N53 (≠ D59), V54 (= V60), N80 (≠ C85), A81 (= A86), G82 (= G87), I130 (≠ T145), S132 (= S147), Y145 (= Y160), K149 (= K164), P177 (= P190), G178 (= G191), I180 (≠ F193), T182 (= T195)
Query Sequence
>RR42_RS03005 FitnessBrowser__Cup4G11:RR42_RS03005
MKLANLSAVVTGGASGLGLACARRLAERGVAVVIADLSEENGAAAVQELGALARFVQADV
CDTAQMTRVFDTADTLGTMRALIHCAGVGGPVRLVEKDGQPGSLEKYESIVRINLVGTFN
TLRLAAARMARNELVDGERGACVLTASVAAYEGQIGQIPYASAKAGIVGMTLVAARDLAQ
RMIRVCTIAPGLFDTPLLARLPENVRASLGASVPHPARLGMPDEFASTALHILENAMLNG
ETIRLDGAIRMAPR
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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