SitesBLAST
Comparing GFF4162 Psest_4235 3-hydroxyacyl-CoA dehydrogenase 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)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
51% identity, 98% coverage: 6:695/701 of query aligns to 3:691/692 of 6iunB
- active site: A60 (= A63), F65 (= F68), E73 (≠ A74), H77 (≠ P78), G101 (= G102), E104 (= E105), E124 (= E125), G132 (= G133), K248 (= K252), S407 (= S411), H428 (= H432), E440 (= E444), N478 (= N482)
- binding nicotinamide-adenine-dinucleotide: G300 (= G304), T301 (= T305), M302 (= M306), E321 (= E325), T322 (≠ I326), Y365 (= Y369), A377 (= A381), V378 (= V382), E380 (= E384), V384 (= V388), V388 (= V392), N405 (= N409), S407 (= S411)
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
41% identity, 100% coverage: 1:699/701 of query aligns to 1:714/723 of Q08426
- E3 (≠ D3) to K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- V40 (≠ E42) to G: in dbSNP:rs1062551
- I41 (≠ A43) to R: in dbSNP:rs1062552
- T75 (≠ S76) to I: in dbSNP:rs1062553
- K165 (≠ E166) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ E172) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
- A274 (= A276) to T: in dbSNP:rs2302819
- A325 (≠ L323) to G: in dbSNP:rs1062555
- K346 (≠ T341) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- K584 (vs. gap) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- K598 (≠ P586) to T: in dbSNP:rs1042437
- T606 (≠ E594) to P: in dbSNP:rs1042438
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 11:712/716 of 6z5oAAA
- active site: A67 (= A63), F72 (= F68), G82 (≠ P78), G106 (= G102), E109 (= E105), P128 (= P124), E129 (= E125), G137 (= G133), K255 (= K252), S409 (= S411), H430 (= H432), E442 (= E444), N480 (= N482)
- binding coenzyme a: P26 (= P22), V27 (= V23), A65 (= A61), D68 (= D64), I69 (= I65), P128 (= P124), Y162 (≠ P158), F277 (= F274), K281 (≠ R278)
- binding nicotinamide-adenine-dinucleotide: G309 (= G302), G311 (= G304), T312 (= T305), M313 (= M306), E332 (= E325), S333 (≠ I326), Q337 (≠ A330), A379 (= A381), V380 (= V382), F381 (= F383), E382 (= E384), K387 (= K389), N407 (= N409), S409 (= S411), H430 (= H432)
- binding nicotinamide: A67 (= A63), E109 (= E105), E129 (= E125), P136 (= P132), F261 (= F258)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 11:719/727 of 3zwaA
- active site: A67 (= A63), F72 (= F68), G82 (≠ P78), G106 (= G102), E109 (= E105), P128 (= P124), E129 (= E125), P136 (= P132), G137 (= G133), K255 (= K252), S416 (= S411), H437 (= H432), E449 (= E444), N487 (= N482)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V23), A65 (= A61), G66 (= G62), A67 (= A63), D68 (= D64), I69 (= I65), L104 (= L100), E109 (= E105), R124 (≠ K120), E129 (= E125), L132 (= L128), G137 (= G133), Y162 (≠ P158)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
41% identity, 99% coverage: 7:699/701 of query aligns to 10:716/723 of 6zibAAA
- active site: A66 (= A63), F71 (= F68), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), G136 (= G133), K254 (= K252), S413 (= S411), H434 (= H432), E446 (= E444), N484 (= N482)
- binding acetoacetyl-coenzyme a: P25 (= P22), V26 (= V23), A64 (= A61), G65 (= G62), A66 (= A63), D67 (= D64), I68 (= I65), G104 (= G101), G105 (= G102), E128 (= E125), Y161 (≠ P158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G304), T311 (= T305), M312 (= M306), E331 (= E325), S332 (≠ I326), Q336 (≠ A330), A383 (= A381), V384 (= V382), F385 (= F383), E386 (= E384), N411 (= N409), H434 (= H432)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
41% identity, 99% coverage: 7:699/701 of query aligns to 10:716/723 of 6zicAAA
- active site: A66 (= A63), F71 (= F68), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), G136 (= G133), K254 (= K252), S413 (= S411), H434 (= H432), E446 (= E444), N484 (= N482)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P22), V26 (= V23), A28 (= A25), A66 (= A63), D67 (= D64), I68 (= I65), G104 (= G101), G105 (= G102), E108 (= E105), E128 (= E125), Y161 (≠ P158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G302), G310 (= G304), T311 (= T305), M312 (= M306), E331 (= E325), S332 (≠ I326), Q336 (≠ A330), A383 (= A381), V384 (= V382), F385 (= F383), E386 (= E384), L390 (≠ V388), K391 (= K389), N411 (= N409), S413 (= S411), H434 (= H432)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
41% identity, 99% coverage: 7:699/701 of query aligns to 10:718/725 of 5omoA
- active site: A66 (= A63), F71 (= F68), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (= K252), S415 (= S411), H436 (= H432), E448 (= E444), N486 (= N482)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P22), V26 (= V23), A28 (= A25), P31 (≠ Q28), A64 (= A61), A66 (= A63), D67 (= D64), I68 (= I65), L103 (= L100), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), Y161 (≠ P158), F260 (= F258), K280 (≠ R278)
- binding 3-keto-decanoyl-coa: S415 (= S411), N486 (= N482), K519 (≠ A515), M520 (= M516), V525 (≠ M521), Y658 (= Y642)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 10:718/725 of 5mgbA
- active site: A66 (= A63), F71 (= F68), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (= K252), S415 (= S411), H436 (= H432), E448 (= E444), N486 (= N482)
- binding acetoacetyl-coenzyme a: P25 (= P22), V26 (= V23), A64 (= A61), G65 (= G62), A66 (= A63), D67 (= D64), I68 (= I65), G105 (= G102), E128 (= E125), Y161 (≠ P158)
- binding nicotinamide-adenine-dinucleotide: L307 (≠ I301), G308 (= G302), G310 (= G304), T311 (= T305), M312 (= M306), E331 (= E325), S332 (≠ I326), Q336 (≠ A330), V386 (= V382), F387 (= F383), E388 (= E384), N413 (= N409), S415 (= S411), H436 (= H432)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 10:718/725 of 3zwcA
- active site: A66 (= A63), F71 (= F68), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (= K252), S415 (= S411), H436 (= H432), E448 (= E444), N486 (= N482)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V23), A64 (= A61), G65 (= G62), A66 (= A63), D67 (= D64), I68 (= I65), G77 (≠ A74), L78 (≠ P75), L80 (= L77), V101 (≠ T98), G104 (= G101), G105 (= G102), E108 (= E105), E128 (= E125), F260 (= F258)
- binding nicotinamide-adenine-dinucleotide: G308 (= G302), G310 (= G304), T311 (= T305), M312 (= M306), E331 (= E325), Q336 (≠ A330), A385 (= A381), V386 (= V382), F387 (= F383), E388 (= E384), K393 (= K389), N413 (= N409), S415 (= S411), H436 (= H432)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 10:718/725 of 2x58A
- active site: A66 (= A63), F71 (= F68), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (= K252), S415 (= S411), H436 (= H432), E448 (= E444), N486 (= N482)
- binding adenosine-5'-diphosphate: G310 (= G304), T311 (= T305), M312 (= M306), E331 (= E325), S332 (≠ I326), Q336 (≠ A330), V386 (= V382), L392 (≠ V388)
- binding coenzyme a: V26 (= V23), A28 (= A25), A64 (= A61), A66 (= A63), D67 (= D64), I68 (= I65), E128 (= E125)
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2- methylbutanoyl-coa (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 8:716/723 of 3zw9A
- active site: A64 (= A63), F69 (= F68), G79 (≠ P78), G103 (= G102), E106 (= E105), P125 (= P124), E126 (= E125), P133 (= P132), G134 (= G133), K252 (= K252), S413 (= S411), H434 (= H432), E446 (= E444), N484 (= N482)
- binding nicotinamide-adenine-dinucleotide: L305 (≠ I301), G306 (= G302), G308 (= G304), T309 (= T305), M310 (= M306), E329 (= E325), Q334 (≠ A330), A383 (= A381), V384 (= V382), F385 (= F383), E386 (= E384), N411 (= N409), S413 (= S411), H434 (= H432)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V23), A62 (= A61), G63 (= G62), A64 (= A63), I66 (= I65), G102 (= G101), G103 (= G102), E106 (= E105), E126 (= E125), P133 (= P132), Y159 (≠ P158)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
41% identity, 99% coverage: 7:699/701 of query aligns to 10:718/725 of 3zwbA
- active site: A66 (= A63), G81 (≠ P78), G105 (= G102), E108 (= E105), P127 (= P124), A128 (≠ E125), P135 (= P132), G136 (= G133), S415 (= S411), H436 (= H432), E448 (= E444), N486 (= N482)
- binding (2E)-Hexenoyl-CoA: P25 (= P22), V26 (= V23), A28 (= A25), A64 (= A61), G65 (= G62), A66 (= A63), D67 (= D64), I68 (= I65), V101 (≠ T98), L103 (= L100), G105 (= G102), E108 (= E105), G136 (= G133), Y161 (≠ P158), K280 (≠ R278)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
34% identity, 99% coverage: 5:698/701 of query aligns to 8:704/707 of 6yswA
- active site: A66 (= A63), I71 (≠ F68), A84 (vs. gap), Q88 (≠ P78), G112 (= G102), E115 (= E105), P136 (= P124), E137 (= E125), G145 (= G133), D264 (≠ K252), S422 (= S411), H443 (= H432), E455 (= E444), N493 (= N482)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V23), A66 (= A63), D67 (= D64), I68 (= I65), P136 (= P124), E137 (= E125), L140 (= L128), T290 (≠ R278), K293 (≠ G281)
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
33% identity, 96% coverage: 23:694/701 of query aligns to 29:713/715 of 1wdlA
- active site: A69 (= A63), N89 (vs. gap), N93 (vs. gap), G117 (= G102), E120 (= E105), P139 (= P124), E140 (= E125), P147 (= P132), G148 (= G133), S430 (= S411), H451 (= H432), E463 (= E444), N501 (= N482)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G303), I324 (≠ T305), M325 (= M306), D344 (≠ E325), I345 (= I326), A400 (= A381), V401 (= V382), E403 (= E384), N428 (= N409), T429 (= T410), S430 (= S411)
P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
33% identity, 96% coverage: 23:694/701 of query aligns to 29:713/715 of P28793
P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
31% identity, 96% coverage: 9:684/701 of query aligns to 45:750/763 of P40939
- V282 (≠ L214) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (= I236) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ S273) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E444) active site, For hydroxyacyl-coenzyme A dehydrogenase activity; to Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
33% identity, 96% coverage: 23:694/701 of query aligns to 29:705/707 of 1wdmA
- active site: A69 (= A63), N89 (vs. gap), N93 (vs. gap), G117 (= G102), E120 (= E105), P139 (= P124), E140 (= E125), P147 (= P132), G148 (= G133), S430 (= S411), H451 (= H432), E463 (= E444), N501 (= N482)
- binding acetyl coenzyme *a: K142 (= K127), D297 (≠ E277), M459 (= M440), N501 (= N482), P534 (≠ A515), Y652 (≠ N640), L658 (≠ A646)
- binding nicotinamide-adenine-dinucleotide: G321 (= G302), A322 (≠ G303), I324 (≠ T305), M325 (= M306), D344 (≠ E325), V401 (= V382), E403 (= E384), N428 (= N409), S430 (= S411), N454 (≠ S435)
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
31% identity, 93% coverage: 13:664/701 of query aligns to 17:684/729 of P21177
- G116 (= G102) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
- G322 (= G304) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H432) active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
31% identity, 93% coverage: 13:664/701 of query aligns to 17:684/719 of 6tnmA
- active site: A68 (= A63), F73 (= F68), G116 (= G102), E119 (= E105), P138 (= P124), E139 (= E125), G147 (= G133), N271 (≠ K252), S429 (= S411), H450 (= H432), E462 (= E444), N500 (= N482)
- binding adenosine-5'-triphosphate: D343 (≠ E325), I344 (= I326), V400 (= V382), V401 (≠ F383), V406 (= V388), K584 (= K563)
7o4uA Structure of the alpha subunit of mycobacterium tuberculosis beta- oxidation trifunctional enzyme in complex with oxidized nicotinamide adenine dinucleotide (see paper)
31% identity, 95% coverage: 13:680/701 of query aligns to 13:705/711 of 7o4uA
Query Sequence
>GFF4162 Psest_4235 3-hydroxyacyl-CoA dehydrogenase
MTDVVRLEVQGEIALITVNNPPVNALGQAVREGLQKAFQSAEADPQVRAVALVCEGNTFI
AGADIKEFGKPPQAPSLPEVIEIIEACNKSSVAVIHGTALGGGLEVALGCHYRIARKDAK
VGLPEVKLGLLPGAGGTQRLPRLAGVEKALEMIVSGQPISAAEAVEHNIVDELFEGDLVE
AGLAYVRRMVEEGRTPRRTGEQTQGLEGADNEALIRAKHAEVAKRMPGLFSPLRCIAAVE
AATKLPLAEGLKRERELFAECLNSPQRGALVHSFFAERQAGKINDLPSDTKPRSINSAAV
IGGGTMGVGIALSFANAGVPVKLLEINEEALQRGLQRARDTYAASVKRGSLTEDAMEQRL
ALIEGVTEYAALADADVVVEAVFEEMGVKQQVFEQLDAICKPGAILASNTSSLDLDAIAA
FTKRPEDVVGLHFFSPANVMRLLEVVRGAKTSDEVLATAMAIGKQLKKVSVVVGVCDGFV
GNRMVFQYGREAEFLLEEGATPQQVDAALRNFGMAMGPFAMRDLSGLDIGQAIRKRQRAT
LPAHLDFPTVSDKLCAAGMLGQKTGAGYYRYEPGNRTPQENPDLAPMLEAASLEKGIERK
ALDEQYIVERCIFALVNEGAKILEEGIAQRSSDIDVIYLNGYGFPAFRGGPMFYADSVGL
DRVLARVKELHARCGDWWKPAPLLEKLAAEGRTFTDWQAGQ
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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