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Database: UniProt
Entry: A0A2U4BZS8_TURTR
LinkDB: A0A2U4BZS8_TURTR
Original site: A0A2U4BZS8_TURTR 
ID   A0A2U4BZS8_TURTR        Unreviewed;       763 AA.
AC   A0A2U4BZS8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 2.
DT   27-MAR-2024, entry version 22.
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|RefSeq:XP_019798668.2};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019798668.2};
RN   [1] {ECO:0000313|RefSeq:XP_019798668.2}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019798668.2};
RG   RefSeq;
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   RefSeq; XP_019798668.2; XM_019943109.2.
DR   AlphaFoldDB; A0A2U4BZS8; -.
DR   STRING; 9739.ENSTTRP00000009681; -.
DR   InParanoid; A0A2U4BZS8; -.
DR   OMA; ESTTIRW; -.
DR   OrthoDB; 622692at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000245320; Chromosome 14.
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; 1.
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:UP000245320}.
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   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;  82976 MW;  69557494B8DAB2EA CRC64;
     MVASRAVGSL SRFTASRMLR CPGYICRNFT RSSALLTRTH INYGVKGDVA VIRINSPNSK
     VNTLGQEVHS EFIEVMNEVW SSNQIRSAVL ISSKPGCFIA GADLNMLTAC TTPQEVTQIS
     QEAQRMFEKV EKSTKPIVAA INGSCLGGGL ELAISCQYRI ATKDKKTVLG SPEVLLGILP
     GAGGTQRLPK MVGVPAAFDM MLTGRGIRAD RAKKMGLVDQ LVEPLGPGIK PPEERTIEYL
     EEVAITFAKG LADKKISPKR DKGLVEKLTS YAMSIPFVRQ QIYKKVEERV RKQTKGLYPA
     PLKIIDVVKT GIEQGSDAGY LSESQKFGEL AMTKESKALM GLYRGQTLCK KNKFGAPQKE
     VKQLAILGAG LMGAGIAQVS VDKGLQTILK DATLAALGRG QQQVFRGLND KVKKKALTSF
     ERDAFFSNLT GQLDYQGFEK ADMVIEAVFE DLSLKHKVLK EVEAVIPDHC VFASNTSALP
     INEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTQKTSKD TTASAVEVGL KQGKVIIVVK
     DGPGFYTTRC LAPMMSEVIR ILQEGVGPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA
     ENLGKVFGER FAGGSLEVLK QMIAKGFLGR KSGKGFYIYQ EGVKNKNLNS DIDSILASLK
     MPSQPDVSSD EDIQYRLVTR FVNEAVLCLQ EGVLASPTEG DIGAVFGLGF PPSLGGPFRF
     VDLYGAQKIV DRLRKYEAAY GKQFTPCQLL VDHASSPNKK FYQ
//
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