ID U1JSJ9_9GAMM Unreviewed; 739 AA.
AC U1JSJ9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=fadJ {ECO:0000313|EMBL:ERG28143.1};
GN ORFNames=PMAN_02600 {ECO:0000313|EMBL:ERG28143.1};
OS Pseudoalteromonas marina DSM 17587.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG28143.1, ECO:0000313|Proteomes:UP000016528};
RN [1] {ECO:0000313|EMBL:ERG28143.1, ECO:0000313|Proteomes:UP000016528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
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: 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}.
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:ERG28143.1}.
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DR EMBL; AHCB02000001; ERG28143.1; -; Genomic_DNA.
DR AlphaFoldDB; U1JSJ9; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000016528; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:InterPro.
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; IPR012802; FadJ.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02440; FadJ; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000313|EMBL:ERG28143.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 311..490
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 492..585
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 613..697
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 717..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 80392 MW; 15CCF91D8D073BF1 CRC64;
MTDSVFNLAV DENKIAVVTI DVPGEKMNTL RDSFADDLKA LLTQAQEHAV KGMVFISGKS
DNFIAGADVK MLDSVEKRED ALAISELCHQ AFFDMKKLPY TTVSAIHGAA LGGGLEFALA
CDYRVGTDSD LTKIGLPEVQ LGLLPGGGGT QRLTKIVGIQ KALEWMLTGK QIRPKQAKKA
GVLDDCVPQS VLLKVAKEFA AKKKPQTKEP KLDKVSKLLE SNPFGRNFIF KKAKENVLKK
TGGHYPAPLA IIKAVRASVE LDELKAYKTE AEGFATLVMS EQSKALRGLF FATTEMKKEW
RNDDAPAVTK TAVLGGGLMG AGIAHVSAVK AKVPVRIKDV AEQGISNAMN YTYKILDKRL
KRRIMSKADM QLTMNRITGT TDYSGFKHID LVIEAVFEDL ALKQGMVADV EQQCQENTIF
ASNTSSLPIS QIAANATRPE NVIGLHYFSP VEKMPLVEII PHEGTSQETI ARVVNFARKQ
GKTPIVVKDM AGFYVNRILA PYLNEAANLM LAGEPIEKID AALVEFGFPV GPLALLDEVG
IDIGSKIAPI LEKELGERFK GPDAFSRMID SKRLGRKTGR GFYDYEKKGK KVDESVYELL
GVTPNSRLNK SEIAQRCVAQ MLNEAARCLD EGIIASPRDG DIGAIFGIGF PPFLGGPFSY
MDKLGTSKVS SDMSTLANSN AIFAPCESLV SMAESGETFY GEKPTQNETV AEVVKLETSE
QEADVVPEEQ SDVAKDDTK
//
