ID A0A2K6FY99_PROCO Unreviewed; 763 AA.
AC A0A2K6FY99;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=HADHA {ECO:0000313|Ensembl:ENSPCOP00000018962.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000018962.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000018962.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616;
CC Evidence={ECO:0000256|ARBA:ARBA00001391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188;
CC Evidence={ECO:0000256|ARBA:ARBA00001391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000256|ARBA:ARBA00000193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC Evidence={ECO:0000256|ARBA:ARBA00000193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31163, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000256|ARBA:ARBA00000469};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165;
CC Evidence={ECO:0000256|ARBA:ARBA00000469};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR RefSeq; XP_012507943.1; XM_012652489.1.
DR AlphaFoldDB; A0A2K6FY99; -.
DR STRING; 379532.ENSPCOP00000018962; -.
DR Ensembl; ENSPCOT00000029607.1; ENSPCOP00000018962.1; ENSPCOG00000021407.1.
DR GeneID; 105816928; -.
DR KEGG; pcoq:105816928; -.
DR CTD; 3030; -.
DR GeneTree; ENSGT00940000154677; -.
DR OMA; ESTTIRW; -.
DR OrthoDB; 622692at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR012803; Fa_ox_alpha_mit.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02441; fa_ox_alpha_mit; 1.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 2.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT DOMAIN 364..541
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 544..639
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 676..753
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT ACT_SITE 510
FT /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-1"
FT SITE 151
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 173
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 498
FT /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
SQ SEQUENCE 763 AA; 82979 MW; 6C481B3ACFB20219 CRC64;
MVASRAIGSL SRFTAFRILR SRGYICRNFA GSSALLTRTH INYGVKGDVA VIRINSPNSK
VNTLSKELHS EFLEVMDEIW ASDKIRSAVL ISSKPGCFVA GADVNMLAAC KTPQEVTQIS
QDAQKTFEKL EKSTKPIVAA ISGSCLGGGL ELAISCQYRI ATKDRKTVLG APEVLLGLLP
GAGGTQRLPK MVGVPAAFDM MLTGRNIRAD RAKKMGLVDQ LVDPLGPGLK PPEERTIEYL
EEVAVTFAKG LADKKISPKR DKGLVEKLTA YAMTIPFVRQ QIYKKVEERV RKQTKGLYPA
PLKIIDVVKT GIEQGNDAGY LSESQKFGEL AMTKESKALI GLYYGQVLCK KNKFGAPQKD
VKHLAILGAG LMGAGIAQVS VDKGLKTILK DAAVTGLSRG QQQVFKGLND KVKKKALTSF
ERDAIFSNLT GQLDYRGFEK ADMVIEAVFE DLSLKHKVLK EVEAVIPDHC VFASNTSALP
IGEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD TTASAVAVGL KQGKVIIVVK
DGPGFYTTRC LAPMMSEVIR ILQEGVDPKK LDSLTTGFGF PVGAATLVDE VGVDVAKHVA
EDLGKTFGER FAGGSLELLQ QMVSKGFLGR KSGKGFYIYQ EGVKNKNLNS DMDSIFATLK
LPPKSEVSSD EDIQYRLVTR FVNEAVMCLQ EGILATPAEG DIGAVFGLGF PACLGGPFRF
LDLYGAQKIV DRLRRYEDAY GKQFTPCQLL MDHASSPNKK FYP
//
