ID A0A2K5DSL0_AOTNA Unreviewed; 757 AA.
AC A0A2K5DSL0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSANAP00000023872.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000023872.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000023872.1}
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 AlphaFoldDB; A0A2K5DSL0; -.
DR STRING; 37293.ENSANAP00000023872; -.
DR Ensembl; ENSANAT00000041787.1; ENSANAP00000023872.1; ENSANAG00000029684.1.
DR GeneTree; ENSGT00940000154677; -.
DR OMA; ESTTIRW; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000233020; 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:UP000233020}.
FT DOMAIN 358..535
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 538..633
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 670..749
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT ACT_SITE 504
FT /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-1"
FT SITE 145
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 167
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 492
FT /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
SQ SEQUENCE 757 AA; 82353 MW; E3CF5F89A1C4DAAC CRC64;
MVACRAIGIL GRFSAFRILR SRGYICRNFT ESSALLTRTH INYGVKGDVA VIRINSPNSK
VSHLISAIQS SIEIMNKSWP SDSIRSCRTY LIKAQAALFM LAACKTPQEV TQISQEAQRT
FEKLEKSTKP VVAAISGSCL GGGLELAISC QYRIATKDRK TVLGSPEVLL GILPGAGGTQ
RLPKMVGVPA AFDMMLTGRN IRADRAKKMG LVDQLVEPLG PGLKPPEERT IEYLEEVAIT
FAKGLADKKI SPKRDKGLVE KLTAYAMTVP FVRQQVYKKV EEKVRKQTKG LYPAPLKIID
VVKTGIEQGS DAGYLSESQK FGELAMTKES KALMGLYHGQ VLCKKNKFGA PQKDVKHLAI
LGAGLMGAGI AQVSVDKGLK TILKDATLTG LGRGQQQVFK GLNDKVKKKA LTSFERDSIF
SNLTGQLDYQ GFEKADMVIE AVFEDLSLKH RVLKEVEAVI PDHCVFASNT SALPISEIAA
VSKRPEKVIG MHYFSPVDKM QLLEIITTEK TSKDTSASAV AVGLKQGKVI IVVKDGPGFY
TTRCLAPMMS EVIRILQEGV DPKKLDSLTT SFGFPVGAAT LVDEVGVDVA KHVAEDLGKA
FGERFGGGNP ELLTQMVSKG FLGRKSGKGF YIYQEGVKSK NLNSDMDSIL ASLKIPPKSE
VSSDEDIQFR LVTRFVNEAV MCLQEGILAT PAEGDIGAVF GLGFPPCLGG PFRFVDLYGA
QKLVDRLKKY EAAYGKQFTP CQLLADHANS PNKKFYQ
//
