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Database: UniProt
Entry: A0A3Q1NDR1_BOVIN
LinkDB: A0A3Q1NDR1_BOVIN
Original site: A0A3Q1NDR1_BOVIN 
ID   A0A3Q1NDR1_BOVIN        Unreviewed;       771 AA.
AC   A0A3Q1NDR1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSBTAP00000069645.1,
GN   ECO:0000313|VGNC:VGNC:49553};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000069645.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000069645.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069645.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000069645.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069645.1};
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A3Q1NDR1; -.
DR   SMR; A0A3Q1NDR1; -.
DR   STRING; 9913.ENSBTAP00000069645; -.
DR   Ensembl; ENSBTAT00000081101.1; ENSBTAP00000069645.1; ENSBTAG00000015038.6.
DR   VEuPathDB; HostDB:ENSBTAG00000015038; -.
DR   VGNC; VGNC:49553; HADHA.
DR   GeneTree; ENSGT00940000154677; -.
DR   InParanoid; A0A3Q1NDR1; -.
DR   Reactome; R-BTA-1482798; Acyl chain remodeling of CL.
DR   Reactome; R-BTA-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
DR   Reactome; R-BTA-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
DR   Reactome; R-BTA-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR   Reactome; R-BTA-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR   Reactome; R-BTA-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR   Reactome; R-BTA-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000015038; Expressed in omental fat pad and 103 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1NDR1; baseline and differential.
DR   GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IBA:GO_Central.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR   GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1NDR1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN          372..549
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          552..647
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          684..763
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   ACT_SITE        518
FT                   /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-1"
FT   SITE            160
FT                   /note="Important for long-chain enoyl-CoA hydratase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT   SITE            182
FT                   /note="Important for long-chain enoyl-CoA hydratase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT   SITE            506
FT                   /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
SQ   SEQUENCE   771 AA;  84581 MW;  D8A4E4F8AAFAA516 CRC64;
     LRVGHDLAPE QQATNRNSVL KIINCEIRFL TGYICRSFTR SSALLTRTHI NYGVRGDVAV
     IRINSPNSKV NTLSQELHSE FMEVMNEVWS SSQIRSAVLI STKPGCFIAG ADLNMLNSCT
     TSQEVTQISQ EAQKMFEKLE KSTKPVVAAI NGSCLGGGLE LAISCQYRIA TKDKKTVLGS
     PEVLLGILPG AGATQRLPKM VGIPAAFDMM LTGRGIRADR AKKMGLVDQL VEPLGPGVKP
     PEERTIEYLE EVAITFAKGL ADKKITPKRD KGLVEKLTSY ALSIPFVRQQ IYKKVEEKVR
     KQTKGLYPAP LKIIDVSLYP ILQHLSCFFP LSRTFGELAM TKESKALMGL YRGQTQCKKN
     KFGAPQKEVK QLAVLGAGLM GAGIAQVSVD KGLQTILKDT TLPALGRGQQ QVFKGLNDKV
     KKKTLTSFER DAMFSNLIGQ LDYRGFEKAD MVIEAVFEDL NLKHRVLKEA EAVIPDHCVF
     ASNTSALPIG EIATVSKRPE KVIGMHYFSP VDKMQLLEII TTEKTSKDTT ASAVDVGLRQ
     GKVIIVVKDG PGFYTTRCLT PMMSEVIRIL QEGVGPKKLD SLTTSFGFPV GAATLVDEVG
     VDVAKHVAEN LGKEFGERFA GGSLEMLQQM ISKGFLGRKS GKGFYIYQEG VKNKNLNSDM
     DSILASLKMP SQPDVSSDED IQYRLVTRFV NEAILCLQEG VLATPTEGDI GAVFGLGFPP
     CLGGPFHFVD LYGAQKIVDR LRKYEAAYGK QFTPCQLLVD HANNPNKKFY Q
//
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