SitesBLAST
Comparing Pf1N1B4_4785 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4785 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
66% identity, 100% coverage: 1:253/253 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
62% identity, 100% coverage: 1:253/253 of query aligns to 4:255/255 of 4xgnA
- active site: Y161 (= Y159), K165 (= K163)
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (≠ M37), C59 (≠ A56), D60 (= D57), V61 (≠ I58), C86 (= C84), A87 (= A85), V113 (= V111), T146 (= T144), Y161 (= Y159), K165 (= K163), P191 (= P189), I193 (= I191), F194 (= F192), T196 (= T194), M198 (= M196)
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)
54% identity, 98% coverage: 3:250/253 of query aligns to 2:253/255 of O18404
- L33 (= L34) mutation to Q: Lethal allele.
- F120 (= F117) mutation to I: Lethal allele.
- Q159 (= Q156) 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 (= S160) 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)
54% identity, 98% coverage: 3:250/253 of query aligns to 2:253/255 of 1u7tA
- active site: G15 (= G16), N115 (= N112), T147 (= T144), S149 (= S146), Y162 (= Y159), K166 (= K163), F195 (= F192)
- 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 (≠ M37), D58 (= D57), V59 (≠ I58), C85 (= C84), A86 (= A85), G87 (= G86), A89 (≠ V88), V90 (≠ R89), A91 (≠ G90), T147 (= T144), S149 (= S146), Q156 (= Q153), Q159 (= Q156), Y162 (= Y159), K166 (= K163), P192 (= P189), L194 (≠ I191), F195 (= F192), T197 (= T194), L199 (≠ M196), L200 (≠ M197), L203 (≠ M200)
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)
54% identity, 98% coverage: 3:250/253 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 (= D57) binding
- V65 (≠ I58) binding ; to A: in HSD10MD; uncertain significance; dbSNP:rs104886492
- D86 (≠ N79) 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
- R130 (= R121) 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 (= S146) binding
- Q165 (= Q156) 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 (= Y159) active site, Proton acceptor; binding
- K172 (= K163) 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 (= V167) to M: in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing
- F201 (= F192) binding
- T203 (= T194) binding
- P210 (≠ T201) to S: in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization
- K212 (≠ E203) 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 (= R217) 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 (= N238) 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 (= E240) 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)
54% identity, 98% coverage: 3:250/253 of query aligns to 2:253/255 of 8cbkC
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), L36 (≠ M37), D58 (= D57), V59 (≠ I58), C85 (= C84), A86 (= A85), G87 (= G86), T147 (= T144), S149 (= S146), Y162 (= Y159), P192 (= P189), G193 (= G190), T197 (= T194), L199 (≠ M196)
- binding : S92 (≠ E91), K93 (= K92)
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, 98% coverage: 3:250/253 of query aligns to 8:259/261 of O70351
- S155 (= S146) binding
- Y168 (= Y159) active site, Proton acceptor
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
52% identity, 98% coverage: 3:250/253 of query aligns to 2:253/255 of 1e3wD
- active site: G15 (= G16), N115 (= N112), T147 (= T144), S149 (= S146), Y162 (= Y159), K166 (= K163), F195 (= F192)
- binding acetoacetic acid: Y162 (= Y159), T202 (≠ G199)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ M37), N58 (≠ D57), V59 (≠ I58), C85 (= C84), A86 (= A85), G87 (= G86), V114 (= V111), T147 (= T144), Y162 (= Y159), K166 (= K163), P192 (= P189), L194 (≠ I191), F195 (= F192), T197 (= T194), L199 (≠ M196)
1uayA Crystal structure of type ii 3-hydroxyacyl-coa dehydrogenase from thermus thermophilus hb8
57% identity, 97% coverage: 9:253/253 of query aligns to 5:241/241 of 1uayA
- active site: G12 (= G16), S134 (= S146), Y147 (= Y159), K151 (= K163)
- binding adenosine: G8 (= G12), S11 (= S15), D32 (= D36), L33 (≠ M37), D46 (= D57), V47 (≠ I58), A73 (= A85), G74 (= G86)
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, 98% coverage: 3:250/253 of query aligns to 8:259/261 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)
52% identity, 98% coverage: 3:250/253 of query aligns to 2:246/248 of 1e6wC
- active site: G15 (= G16), N115 (= N112), T147 (= T144), S149 (= S146), Y162 (= Y159), K166 (= K163), F195 (= F192)
- binding estradiol: Q159 (= Q156), Y162 (= Y159), L200 (≠ M197)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ M37), N58 (≠ D57), V59 (≠ I58), C85 (= C84), A86 (= A85), T147 (= T144), Y162 (= Y159), K166 (= K163), P192 (= P189), L194 (≠ I191), F195 (= F192), T197 (= T194), L199 (≠ M196)
6ujkA Crystal structure of a probable short-chain type dehydrogenase/reductase (rv1144) from mycobacterium tuberculosis with bound NAD
52% identity, 100% coverage: 1:253/253 of query aligns to 2:246/246 of 6ujkA
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), S16 (= S15), G17 (= G16), L18 (= L17), D37 (= D36), L38 (≠ M37), D57 (= D57), V58 (≠ I58), C83 (= C84), A84 (= A85), T142 (= T144), S144 (= S146), Y157 (= Y159), K161 (= K163), G188 (= G190), F190 (= F192), T192 (= T194), L194 (≠ M196)
7n09A Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum
55% identity, 97% coverage: 7:252/253 of query aligns to 10:259/259 of 7n09A
- binding nicotinamide-adenine-dinucleotide: G15 (= G12), S18 (= S15), G19 (= G16), L20 (= L17), D39 (= D36), L40 (≠ M37), S62 (= S59), V63 (≠ N60), C89 (= C84), A90 (= A85), S153 (= S146), Y166 (= Y159), K170 (= K163), P196 (= P189), G197 (= G190), I198 (= I191), F199 (= F192), T201 (= T194), M203 (= M196)
3ppiA Crystal structure of 3-hydroxyacyl-coa dehydrogenase type-2 from mycobacterium avium (see paper)
41% identity, 100% coverage: 2:253/253 of query aligns to 4:258/258 of 3ppiA
4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 98% coverage: 2:250/253 of query aligns to 4:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N112), S139 (= S146), Q149 (= Q156), Y152 (= Y159), K156 (= K163)
- binding acetoacetyl-coenzyme a: D93 (≠ E91), K98 (= K96), S139 (= S146), N146 (≠ Q153), V147 (≠ I154), Q149 (= Q156), Y152 (= Y159), F184 (≠ I191), M189 (= M196), K200 (≠ S207)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ M37), V59 (≠ A56), D60 (= D57), V61 (≠ I58), N87 (≠ C84), A88 (= A85), G89 (= G86), I90 (= I87), T137 (= T144), S139 (= S146), Y152 (= Y159), K156 (= K163), P182 (= P189), F184 (≠ I191), T185 (≠ F192), T187 (= T194), M189 (= M196)
1iy8A Crystal structure of levodione reductase (see paper)
36% identity, 97% coverage: 2:246/253 of query aligns to 1:252/258 of 1iy8A
- active site: G15 (= G16), S143 (= S146), Q153 (= Q156), Y156 (= Y159), K160 (= K163)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (≠ M37), A62 (= A56), D63 (= D57), V64 (≠ I58), N90 (≠ C84), G92 (= G86), I93 (= I87), T141 (= T144), S143 (= S146), Y156 (= Y159), K160 (= K163), P186 (= P189), G187 (= G190), T191 (= T194), P192 (= P195), M193 (= M196)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
36% identity, 97% coverage: 2:246/253 of query aligns to 10:261/267 of Q9LBG2
- 17:42 (vs. 9:34, 65% identical) binding
- E103 (≠ L94) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
33% identity, 99% coverage: 1:251/253 of query aligns to 3:245/245 of 5t5qC
- active site: G18 (= G16), S140 (= S146), N150 (≠ Q156), Y153 (= Y159), K157 (= K163)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ A14), G17 (≠ S15), G18 (= G16), I19 (≠ L17), D38 (= D36), L39 (≠ M37), D63 (≠ E61), A64 (= A62), S90 (≠ C84), I113 (≠ V111), Y153 (= Y159), K157 (= K163), P182 (= P189), I185 (≠ F192), T187 (= T194), M189 (= M196)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
35% identity, 96% coverage: 3:246/253 of query aligns to 3:243/248 of 6ixmC
- active site: G16 (= G16), S142 (= S146), Y155 (= Y159), K159 (= K163)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (= S15), G16 (= G16), I17 (≠ L17), D36 (= D36), I37 (≠ M37), A61 (= A56), D62 (= D57), T63 (≠ I58), N89 (≠ C84), A90 (= A85), M140 (≠ T144), S142 (= S146), Y155 (= Y159), K159 (= K163), P185 (= P189), A186 (≠ G190), Y187 (≠ I191), I188 (≠ F192), L192 (≠ M196)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
34% identity, 98% coverage: 1:248/253 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 (≠ M37), C63 (≠ A56), I65 (= I58), N91 (≠ C84), G93 (= G86), I94 (= I87), V114 (= V111), Y155 (= Y159), K159 (= K163), I188 (≠ F192), T190 (= T194), T193 (≠ M197)
Query Sequence
>Pf1N1B4_4785 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4785
MQIENKVFLVTGGASGLGAATAEMLVAAGAKVMLVDMNAEAVAAQAARLGAQSVVADISN
EAAAQAAVQATVKAFGGLNGLVNCAGIVRGEKILGKNGPHALDSFSQVINVNLIGSFNML
RLAATAIAETEADEDGERGVIINTASAAAFDGQIGQAAYSASKGAIVSLTLPAARELARF
GIRVMTIAPGIFETPMMAGMTPEVRESLAAGVPFPPRLGKASEYAALVRHIIENSMLNGE
VIRLDGALRMAAK
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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