ID A0A418SYF6_9RHOB Unreviewed; 688 AA.
AC A0A418SYF6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=D3P04_08885 {ECO:0000313|EMBL:RJE85977.1};
OS Paracoccus onubensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1675788 {ECO:0000313|EMBL:RJE85977.1, ECO:0000313|Proteomes:UP000284202};
RN [1] {ECO:0000313|Proteomes:UP000284202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1011MAR3C25 {ECO:0000313|Proteomes:UP000284202};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA Laiz L., Saiz-Jimenez C.;
RT "Acidovorax cavernicola nov. sp. isolated from Gruta de las Maravillas
RT (Aracena, Spain).";
RL Submitted (SEP-2018) 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:RJE85977.1}.
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DR EMBL; QZCG01000005; RJE85977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418SYF6; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000284202; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; 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; 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.
DR PROSITE; PS00067; 3HCDH; 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000284202}.
FT DOMAIN 321..495
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 498..592
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 587..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 74025 MW; 18797E9CAF449C84 CRC64;
MANKVLDFLD KSKLELGPPG TAAAHHWRQA EDDGIVWLVL DCPDSPVNIV SEEVLTGLDA
ALRKLAETVP RALVIRSAKP GGFAAGADID SFDRISGESA IRLLEQGHAV LDRLEALPCP
TIAVIHGAAL GAGFEIALAC DHRIAIDGAK FAFPEVNLGL HPGLGGTFRL TGLIDPVEAM
TLMLTGKSAH TQKAKKLGIV DIVTQERHVR AAVGAVVDGK IDPPAKGLKA RAFALRKLRS
LAAARMRAEA EKKAPPAHFP APYALIDLWE IHGNDPEAMQ KAEIASFAGL LDSETSRNLR
RVFFLRRSLK KDGGGDDGIS HVHVIGAGEM GAGIAGWAAI RGKRVTLGDI SPEALARAIR
QVAQICRDSH LNSIETRDAL DRLMPDPKGY GYAGADLVIE AVPEDADLKA KIHREAGARM
KPGAILATNT SSLALAELAK SVPDPARFAG LHFFNPVAKM QLVEIVSHDR TAPDTADRLA
AFCASIDRLP AALRDYPGFL VNRALTPYLM EAMVLMDEGV PKVVIDRAAL DFGMPMGPVT
LADQVGLDIC LDVAESLKSA LDKPMPDISP RLREKVEAGE TGKKAGRGFY DWSNGAPHPQ
ATEAGPEDLQ DRLILPMLDA CMECLRMNVV RNADQVDGAM IFATGFAPFR GGPMHYARTR
GFDRIRDRLA ELADRHGERF RPDPGWDE
//
