ID A0A1G7XQL1_9RHOB Unreviewed; 698 AA.
AC A0A1G7XQL1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SDG86489.1};
GN ORFNames=SAMN04489759_11328 {ECO:0000313|EMBL:SDG86489.1};
OS Sulfitobacter delicatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=218672 {ECO:0000313|EMBL:SDG86489.1, ECO:0000313|Proteomes:UP000199399};
RN [1] {ECO:0000313|EMBL:SDG86489.1, ECO:0000313|Proteomes:UP000199399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16477 {ECO:0000313|EMBL:SDG86489.1,
RC ECO:0000313|Proteomes:UP000199399};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- 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}.
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DR EMBL; FNBP01000013; SDG86489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7XQL1; -.
DR STRING; 218672.SAMN04489759_11328; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000199399; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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: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; 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; 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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 292..468
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 473..566
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 602..687
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 698 AA; 75407 MW; 255BFF44E5ACF55A CRC64;
MTDKIAYSRH DDIVVLRIEN PPVNALSQAV RQGLAEGMDR AEAEDGVRAV MIVGEGRAFI
AGADITEFGK PPMEPHLPNL CNRIEASPLL VVASMHGVSL GGGLEVALSA HYRIAQPSAR
VGLPEVHLGL IPGAGGTQRL PRLIGVEPAL DAITTGRHIK APQALEMGIV DRVEEGDPQE
VGLAYVRELL DSGAERRPIC DMPAPAPIDW DAAYEATLKK GRGQISPAEA VRAVQAGVEK
PFEEGMKAER RIFSELMNTD QRQGMIHAFF SERAVSNLPE LKGVEPRDLK AIGVIGGGTM
GAGIATAALL SGFSVVLIEM KDEAAKAAHE RISGNLQGAL KRGKIDQAKF DKLTGTALAV
STKYDSLSDV DLVVEAVFED MDVKKQVFGK LDAVCKPGCV LASNTSYLDV DEIAASTSRP
GDVIGLHFFS PAHVMKLLEV VVADKTAPEV VATGFALGKA LGKISVRAGV CDGFIGNRIL
ATYRTAADHM VLDGASPYKI DAALEKFGFA MGPFAVADLA GLDIGWATRK RKAATRHPEE
RVPTYIDRLC EQGHFGQKTG QGYYIYEKGK RGGTPNPEIT RLIEEEQKER GITPREFTEA
EIVRRYMCAM VNEAAKVLEE GIAKRPLDID MTLLFGYGFP RYWGGPMKWA DIQGLPNVLA
AIVGFAEQDP WFWKPAPLLA ELVKTNRNFD DLNKEAAK
//
