ID L0WJH1_9GAMM Unreviewed; 719 AA.
AC L0WJH1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=A11A3_00735 {ECO:0000313|EMBL:EKF75975.1};
OS Alcanivorax hongdengensis A-11-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF75975.1};
RN [1] {ECO:0000313|EMBL:EKF75975.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF75975.1};
RX PubMed=23209226; DOI=10.1128/JB.01849-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT hongdengensis Type Strain A-11-3.";
RL J. Bacteriol. 194:6972-6972(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: 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:EKF75975.1}.
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DR EMBL; AMRJ01000001; EKF75975.1; -; Genomic_DNA.
DR RefSeq; WP_008927338.1; NZ_AMRJ01000001.1.
DR AlphaFoldDB; L0WJH1; -.
DR STRING; 1177179.A11A3_00735; -.
DR PATRIC; fig|1177179.3.peg.140; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000010164; 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; 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.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 325..502
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 505..598
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 629..713
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 719 AA; 77322 MW; 2CC3E304331BDFCC CRC64;
MTQSRAFTVK PLDNGVAVLE INVPGDAQNT LKAEFADDFN AAFSDIESAR PKALVLYSTK
PGSFMAGADI NLFEKAENAQ QVSDLSTLCQ QTFGKLETLG IPVVAAIKGA CLGGGLELAL
ACSYRIAANS GDTVLGLPEV MLGLLPAGGG TQRLPRLVGI ASALDMMLTG RQLKARPARK
MGLVDEVVDA VAVYDRAVAR AAQLAGEKDD AGISLGDYFS REGLTKAALE QNSLGRKVVF
DQARKQAAKK THGLYPAPPA IIDAVEAGYE NGLAQGYATE ARLFGELAMS SQSKQLRGIF
HATNTLKKET FVADGVQARQ IHRTGVLGAG LMGAGIALTT VNKAKLPVRL KDRDDKGLAH
GVQYLRDFYN KRVKKGAMSA ADASAELGRA SFTSDYSGFK GLDLVVEAVF EDVKLKHLML
KDVEEHGNDQ TIFASNTSSI PITEIARAAK RPQNVIGLHY FSPVEKMPLL EIITTDQTDP
AVTAGCVAFG KAQGKTVIVV KDGPGFYTTR ILAPYLNEAT RLLTEGVDVK QVDQALVRFG
FPVGPITLLD EVGVDVGTKV GPVLEKAFGE RMASPDAAGL MIENNYLGRK SGRGFYIYEG
VAKGEKPVNT ALYELMNVTT SRDADDEEIV SRCLWMMINE AAYCLQEGII SEPMHGDIGA
IFGLGFPPFR GGPFRYMDSL GLVNAVRTLE RLTEQYGERF KPAPILIDMA KKKARFYQD
//
