SitesBLAST
Comparing GFF2399 FitnessBrowser__psRCH2:GFF2399 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)
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
69% identity, 100% coverage: 1:255/255 of query aligns to 7:261/261 of 4o5oB
Sites not aligning to the query:
4xgnA Crystal structure of 3-hydroxyacyl-coa dehydrogenase in complex with NAD from burkholderia thailandensis
65% 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 (≠ A58), D60 (= D59), V61 (≠ I60), C86 (= C86), A87 (= A87), V113 (≠ I113), T146 (= T146), Y161 (= Y161), K165 (= K165), P191 (= P191), I193 (≠ V193), F194 (= F194), T196 (= T196), M198 (= M198)
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)
53% 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.
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
60% 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 (≠ I60), A73 (= A87), G74 (= G88)
1u7tA Crystal structure of abad/hsd10 with a bound inhibitor (see paper)
53% identity, 98% coverage: 3:252/255 of query aligns to 2:253/255 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 (≠ I60), C85 (= C86), A86 (= A87), G87 (= G88), A89 (= A90), V90 (≠ G91), A91 (≠ G92), T147 (= T146), S149 (= S148), Q156 (= Q155), Q159 (= Q158), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ V193), F195 (= F194), T197 (= T196), L199 (≠ M198), L200 (≠ M199), L203 (≠ M202)
7onuC Structure of human mitochondrial rnase p in complex with mitochondrial pre-tRNA-tyr (see paper)
53% identity, 98% coverage: 3:252/255 of query aligns to 2:253/255 of 7onuC
- binding nicotinamide-adenine-dinucleotide: S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (= L37), V59 (≠ I60), C85 (= C86), S149 (= S148), Y162 (= Y161), F195 (= F194), T197 (= T196)
- 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)
53% identity, 98% coverage: 3:252/255 of query aligns to 8:259/261 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 (= D59) binding
- V65 (≠ I60) binding ; 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
- 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
- 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
- K172 (= K165) 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 (= V169) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (= F194) binding
- T203 (= T196) binding
- P210 (≠ T203) 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
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
51% identity, 98% coverage: 3:252/255 of query aligns to 2:253/255 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 (≠ I60), C85 (= C86), A86 (= A87), G87 (= G88), V114 (≠ I113), T147 (= T146), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ V193), F195 (= F194), T197 (= T196), L199 (≠ M198)
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)
51% identity, 98% coverage: 3:252/255 of query aligns to 8:259/261 of O70351
- S155 (= S148) binding
- Y168 (= Y161) active site, Proton acceptor
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)
51% identity, 98% coverage: 3:252/255 of query aligns to 8:259/261 of O08756
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
2o23B The structure of wild-type human hadh2 (17beta-hydroxysteroid dehydrogenase type 10) bound to NAD+ at 1.2 a
53% identity, 98% coverage: 3:252/255 of query aligns to 8:251/255 of 2o23B
- active site: G21 (= G16), N121 (= N114), T153 (= T146), S155 (= S148), Y168 (= Y161), K172 (= K165), F201 (= F194)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), S20 (= S15), G21 (= G16), L22 (= L17), D41 (= D36), L42 (= L37), D64 (= D59), V65 (≠ I60), C91 (= C86), A92 (= A87), T153 (= T146), Y168 (= Y161), K172 (= K165), P198 (= P191), L200 (≠ V193), F201 (= F194), T203 (= T196), L205 (≠ M198)
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
51% identity, 98% coverage: 3:252/255 of query aligns to 2:246/248 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 (≠ M199)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ L37), N58 (≠ D59), V59 (≠ I60), C85 (= C86), A86 (= A87), T147 (= T146), Y162 (= Y161), K166 (= K165), P192 (= P191), L194 (≠ V193), F195 (= F194), T197 (= T196), L199 (≠ M198)
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
54% 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 (≠ I60), C83 (= C86), A84 (= A87), T142 (= T146), S144 (= S148), Y157 (= Y161), K161 (= K165), G188 (= G192), F190 (= F194), T192 (= T196), L194 (≠ M198)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
50% 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 (≠ I60), C89 (= C86), A90 (= A87), S153 (= S148), Y166 (= Y161), K170 (= K165), P196 (= P191), G197 (= G192), I198 (≠ V193), F199 (= F194), T201 (= T196), M203 (= M198)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
40% 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 (≠ E93), K98 (≠ R98), S139 (= S148), N146 (≠ Q155), V147 (≠ I156), Q149 (= Q158), Y152 (= Y161), F184 (≠ V193), M189 (= M198), K200 (≠ S209)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ L37), V59 (≠ A58), D60 (= D59), V61 (≠ I60), N87 (≠ C86), A88 (= A87), G89 (= G88), I90 (≠ V89), T137 (= T146), S139 (= S148), Y152 (= Y161), K156 (= K165), P182 (= P191), F184 (≠ V193), T185 (≠ F194), T187 (= T196), M189 (= M198)
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
34% identity, 98% coverage: 2:252/255 of query aligns to 3:248/248 of 4cqmA
- active site: G17 (= G16), S143 (= S148), Y156 (= Y161), K160 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), S16 (= S15), G17 (= G16), I18 (≠ L17), D37 (= D36), L38 (= L37), A61 (= A58), V63 (≠ I60), C90 (= C86), A91 (= A87), G92 (= G88), I93 (≠ V89), V113 (≠ I113), I141 (≠ T146), S143 (= S148), Y156 (= Y161), K160 (= K165), P186 (= P191), G187 (= G192), I189 (≠ F194), T191 (= T196), P192 (= P197), M193 (= M198), T194 (≠ M199)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
36% identity, 97% coverage: 1:248/255 of query aligns to 3:250/255 of 5itvA
- active site: G18 (= G16), S141 (= S148), Y154 (= Y161), K158 (= K165)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (= S15), G18 (= G16), I19 (≠ L17), D38 (= D36), I39 (≠ L37), T61 (≠ A58), I63 (= I60), N89 (≠ C86), G91 (= G88), T139 (= T146), S141 (= S148), Y154 (= Y161), K158 (= K165), P184 (= P191), G185 (= G192), I186 (≠ V193), I187 (≠ F194)
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
34% identity, 98% coverage: 2:252/255 of query aligns to 5:251/251 of 4cqlI
- active site: G19 (= G16), S146 (= S148), Y159 (= Y161), K163 (= K165)
- binding nicotinamide-adenine-dinucleotide: S18 (= S15), G19 (= G16), I20 (≠ L17), D39 (= D36), L40 (= L37), A64 (= A58), D65 (= D59), V66 (≠ I60), C93 (= C86), A94 (= A87), G95 (= G88), I96 (≠ V89), V116 (≠ I113), I144 (≠ T146), S146 (= S148), Y159 (= Y161), K163 (= K165), P189 (= P191), G190 (= G192), I192 (≠ F194), T194 (= T196), M196 (= M198)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
33% 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.
Query Sequence
>GFF2399 FitnessBrowser__psRCH2:GFF2399
MQIRDKVFLITGGASGLGAAAAQALVEAGGKVVLADLDEAAANATAQALGPSALGVAADI
HDEQAARHAVATAREHFGGLHGLVNCAGVAGGEKVLGRNGPHSLDAFSRIVGINLIGSFN
MLRLAAEAMAENAPDADGERGAIINTASIAAFDGQIGQAAYAASKGGVVSMTLPAARELA
RFGIRVMTIAPGVFETPMMAGMTQEIRDSLAAGVPFPPRLGHPAEYAALVRHIFENSMLN
GEVIRLDGALRMAAK
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