ID A0A173L134_9SPHN Unreviewed; 581 AA.
AC A0A173L134;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=EP837_03778 {ECO:0000313|EMBL:ANI80158.1};
OS Sphingobium sp. EP60837.
OG Plasmid pep1 {ECO:0000313|Proteomes:UP000078304}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI80158.1, ECO:0000313|Proteomes:UP000078304};
RN [1] {ECO:0000313|EMBL:ANI80158.1, ECO:0000313|Proteomes:UP000078304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EP60837 {ECO:0000313|EMBL:ANI80158.1,
RC ECO:0000313|Proteomes:UP000078304};
RC PLASMID=Plasmid pep1 {ECO:0000313|Proteomes:UP000078304};
RA Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT "Complete genome sequence of a organophosphorus pesticides.";
RL Submitted (JUN-2016) 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 -!- 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}.
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DR EMBL; CP015988; ANI80158.1; -; Genomic_DNA.
DR RefSeq; WP_066532009.1; NZ_CP015988.1.
DR AlphaFoldDB; A0A173L134; -.
DR KEGG; sphb:EP837_03778; -.
DR OrthoDB; 9771883at2; -.
DR Proteomes; UP000078304; Plasmid pep1.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Oxidoreductase {ECO:0000313|EMBL:ANI80158.1};
KW Plasmid {ECO:0000313|EMBL:ANI80158.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078304}.
FT DOMAIN 327..434
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
SQ SEQUENCE 581 AA; 60857 MW; 80C8CF6319F71FD4 CRC64;
MSSGNKSDVV RLEKRDDIGI ITIDNPPINA GARGVRIGLL AAVQAFSEDS GLAAGVLIGA
GRMFMAGSDM REINAPVLDP ILPEVIGAIE RCPKPIVAAI AGAALGGGYE LSLGCDARIA
SPEAVVGLPE CALGMMPGAG GTQRLPRLAG LPVSIRLICS GERVKARRAA EIGMIDKVVD
GPLLEEAIAF ARGLGGRKRR VMEMTAPDCD PADLDRAKVD ALAAGGGRPH IQLAIDAVEW
CRTRPGDEAL REERKIFDRL RTGPEAEAML HLFFAERDSM KDASVDLSSS ASLDHVAIVG
IGPDCDALAA AMVRRGHSVV LVSELSDLDA VSSCDVIFVA EQANDDRIGA LLVRLSAHAR
AHAVVLVAGG GQTVATLEKA FGRSGKLCGW RGMAGAAGSG IVEIVRQART EPRTLATALA
LAKAAGQMAV MVGDSEGLVG RRIAAAAHRS CVLLQEQGVR AEQLREVLTR FGLPVPPLSE
ATRAEPQTTM DDEQIASWIL VAIANEAALM LAAGRVRSPG DVDLLLTNAY GFPRHEGGIG
LWARRQQRAN LKQVVGMLAE ASGERFERAP DVALDALCGE G
//
