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Database: UniProt
Entry: A0A0J9EAW0_9RHOB
LinkDB: A0A0J9EAW0_9RHOB
Original site: A0A0J9EAW0_9RHOB 
ID   A0A0J9EAW0_9RHOB        Unreviewed;       730 AA.
AC   A0A0J9EAW0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Enoyl-CoA hydratase {ECO:0000313|EMBL:KMW59761.1};
DE            EC=1.1.1.35 {ECO:0000313|EMBL:KMW59761.1};
DE            EC=4.2.1.17 {ECO:0000313|EMBL:KMW59761.1};
DE            EC=5.1.2.3 {ECO:0000313|EMBL:KMW59761.1};
GN   ORFNames=AIOL_004744 {ECO:0000313|EMBL:KMW59761.1};
OS   Candidatus Rhodobacter lobularis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW59761.1, ECO:0000313|Proteomes:UP000037178};
RN   [1] {ECO:0000313|EMBL:KMW59761.1, ECO:0000313|Proteomes:UP000037178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGS {ECO:0000313|EMBL:KMW59761.1};
RA   Jourda C., Santini S., Claverie J.-M.;
RT   "Draft genome sequence of an Alphaproteobacteria species associated to the
RT   Mediterranean sponge Oscarella lobularis.";
RL   Submitted (JUN-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 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:KMW59761.1}.
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DR   EMBL; LFTY01000002; KMW59761.1; -; Genomic_DNA.
DR   RefSeq; WP_049645191.1; NZ_LFTY01000002.1.
DR   AlphaFoldDB; A0A0J9EAW0; -.
DR   STRING; 1675527.AIOL_004744; -.
DR   PATRIC; fig|1675527.3.peg.4979; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000037178; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
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.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Isomerase {ECO:0000313|EMBL:KMW59761.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KMW59761.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:KMW59761.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT   DOMAIN          327..505
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          509..604
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   730 AA;  77868 MW;  853F8CB72635E75C CRC64;
     MADFIMTKGD DGVAVITWDV PGKSMNVMSR EAMPLLGNLV DDALADEAVT GIIITSGKKD
     FAGGMDLNVL GSISAEAGDN PAQALFDFTM AGHHGLRKIE RAGMDPKTNK GGKPIACVLP
     GTALGIGFEI PLACHRIFAA DNPKAKIGLP EILVGLFPGA GGTTRLVRKL GAMAASPFLL
     EGKLSDPKKA KAAGLIDEVS EDPMAAAREW VLGATDADIV KPWDAKGYKM PGGMPYHPSG
     FMTFVGAAAM VHGKTQGVYP AAKALLAAAY EGAQVPFETA LKIEARHFTS VLMSPTSSAM
     IRSLFVNKEA LEKGANRPDV ADETVKKVGV LGAGMMGAGI ALVSAQAGIE VVLIDQTQEA
     ADKGRAYTEA YMDKGIARRK ATPEKKEQML ARITATTDLS ALADCDLIVE AVFEDPAVKA
     EMTKKVEAVI PADCIFASNT STLPITELAK ASSRPEQFIG IHFFSPVERM MLVEIIKGAE
     TGDRAVAKSL DYVRQIRKTP IVVNDARFFY ANRCIIPYIN EGVRMVGEGV EPALVENAAK
     MLGFPVGPLQ LNDETSIDLG VKIAKATKAA LGDAYDAGAA DEVLFWLFDQ GRMGRKSSAG
     YYDYDEKGKR TGIWPGLRDK YTKDDHPDLT EVQHRLMMAQ VLEAVRAIEE DVLLDIREGD
     VGAILGWGFA PWSGGPLSWL DMIGATKAVE ICDGLEAKFG KRFAAPALLK DIAAKGESFY
     GRFTETKAAA
//
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