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Database: UniProt
Entry: A0A452FQ66_CAPHI
LinkDB: A0A452FQ66_CAPHI
Original site: A0A452FQ66_CAPHI 
ID   A0A452FQ66_CAPHI        Unreviewed;       753 AA.
AC   A0A452FQ66;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:ENSCHIP00000026372.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000026372.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000026372.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000026372.1}
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   EMBL; LWLT01000009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A452FQ66; -.
DR   SMR; A0A452FQ66; -.
DR   Ensembl; ENSCHIT00000034235.1; ENSCHIP00000026372.1; ENSCHIG00000022677.1.
DR   GeneTree; ENSGT00940000154677; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000291000; Chromosome 11.
DR   Bgee; ENSCHIG00000022677; Expressed in longissimus thoracis muscle and 17 other cell types or tissues.
DR   GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
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: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   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:UP000291000};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..753
FT                   /note="enoyl-CoA hydratase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019460138"
FT   DOMAIN          354..531
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          534..629
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          666..745
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   ACT_SITE        500
FT                   /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-1"
FT   SITE            141
FT                   /note="Important for long-chain enoyl-CoA hydratase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT   SITE            163
FT                   /note="Important for long-chain enoyl-CoA hydratase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT   SITE            488
FT                   /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
SQ   SEQUENCE   753 AA;  82479 MW;  9970AA94B45039AE CRC64;
     RRWLASSILI YFSYICRSFT RASALLTRTH INYGVKGDVA VIRINSPNSK VNTLSQELHS
     EFMEVMNEVW SSSQIRSAVL ISTKPGCFIA GADLNMLNAC TTSQEVTQIS QEAQKMFEKL
     EKSTKPVVAA INGSCLGGGL ELAISCQYRI ATKDKKTVLG SPEVLLGILP GAGATQRLPK
     MVGIPAAFDM MLTGRSIRAD RAKKMGLVDQ LVEPLGPGVK PPEERTIEYL EEVAITFAKG
     LADKKITPKR DKGLVEKMTS YALSIPFVRQ QIYKKVEEKV RKQTKGLYPA PLKIIDVVKT
     GIEQGSNAGY LSESQRFGEL AMTKESKALM GLYRGQTQCK KNKFGAPQKE VKQLAVLGAG
     LMGAGIAQVS VDKGLQTILK DTTLPALGRG QQQVFKGLND KVKKKTLTSF ERDAMFSNLI
     GQLDYRGFEK ADMVIEAVFE DLSLKHRVLK ETEAVIPDHC VFASNTSALP IGEIATVSKR
     PEKVIGMHYF SPVDKMQLLE IITTEKTSKD TTASAVDVGL RQGKVIIVVK DGPGFYTTRC
     LTPMMSEVIR ILQEGVGPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA ENLGKEFGER
     FAGGSLEMLQ QMISKGFLGR KSGKGFYIYQ EGVKNKNLNS DMDSILASLK MPSQPDVSSD
     EDIQYRLVTR FVNEAILCLQ EGVLATPTEG DIGAVFGLGF PPCLGGPFHF VDLYGAQKIV
     DRLRKYEAAY GKQFTPCQLL VDHANNPNKK FYQ
//
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