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Database: UniProt
Entry: A0A0W8J8Y4_9VIBR
LinkDB: A0A0W8J8Y4_9VIBR
Original site: A0A0W8J8Y4_9VIBR 
ID   A0A0W8J8Y4_9VIBR        Unreviewed;       727 AA.
AC   A0A0W8J8Y4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE            EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN   ORFNames=VRK_41160 {ECO:0000313|EMBL:KUI96693.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI96693.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI96693.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI96693.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUI96693.1}.
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DR   EMBL; LQIY01000041; KUI96693.1; -; Genomic_DNA.
DR   RefSeq; WP_059123144.1; NZ_KQ947476.1.
DR   AlphaFoldDB; A0A0W8J8Y4; -.
DR   STRING; 1761910.VRK_41160; -.
DR   PATRIC; fig|1761910.3.peg.4168; -.
DR   OrthoDB; 5389341at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000054473; Unassembled WGS sequence.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:InterPro.
DR   GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase 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; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR02437; FadB; 1.
DR   PANTHER; PTHR43612:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 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.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Isomerase {ECO:0000313|EMBL:KUI96693.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KUI96693.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          318..495
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          497..593
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          627..697
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   727 AA;  80051 MW;  CDC484759141CBBC CRC64;
     MIFQSKTLQV KEIEGGILEL QFCTPLSVNT LDTATLSHLD KALDAIQGFP GLKGLVLTSD
     KESFIVGADI NEFLGLFQYP SDELEQWLHY ANQIFCKLED LPVPTISALC GYTLGGGCEC
     VLATDFRVAA RSTKIGLPET RLGIMPGFGG CVRLPRLIGA DNALEAIVQA KIFSAEHALS
     VGLVDAITTE EALAATARRT LDDAIHNKID WKKARQEKCA PLTLSPVERL MVFSTAKGMT
     HQKVSTHYMA PFLAIETIES SATLSRDEAL NIERKNFVTL AKSDQAAALV SIYLNDQYIK
     GLAKKAKQSL THPVSHSAVI GAGVMGGGIA YQSAIKGIPA VLKDIVPDSL KLGMNHSAQL
     LEQGVKRGKL SPRDMANTLA SIRPTLNYAG IEDVDVIVEA VVENPKIKSS VLKEIEEKVT
     ANTILTSNTS TIPITQLAAG LSRPDKFCGM HFFNPVHKMP LVEIIRGKET SDETIDTVVA
     FAAHMGKSPI VVNDCPGFFV NRVLFPYFLA FCQLLDEGYD FVQIDKIMEK DFGWPMGPAY
     LLDVVGIDIA YHAQQVICQA YPTRMKSSPD NIITRLYEAK KFGQKTGEGF YHYYTDKRGK
     SQKVLSPDIY QLVYASGEPL PVTDKQMIMD RMMIPMMNEV ILCMEENIIS SPAEADIALV
     YGLGFPPFRG GVCRYLDTIG ITQYIQTAQS YQRFGELYHV PKSLEVMAHQ ARVFYPIHHD
     KSESERG
//
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