ID F8CJ36_MYXFH Unreviewed; 746 AA.
AC F8CJ36;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=fadJ {ECO:0000313|EMBL:AEI68818.1};
GN OrderedLocusNames=LILAB_34685 {ECO:0000313|EMBL:AEI68818.1};
OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI68818.1, ECO:0000313|Proteomes:UP000000488};
RN [1] {ECO:0000313|EMBL:AEI68818.1, ECO:0000313|Proteomes:UP000000488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX PubMed=21868801; DOI=10.1128/JB.05516-11;
RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT 1.";
RL J. Bacteriol. 193:5015-5016(2011).
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}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; CP002830; AEI68818.1; -; Genomic_DNA.
DR AlphaFoldDB; F8CJ36; -.
DR STRING; 483219.LILAB_34685; -.
DR KEGG; mfu:LILAB_34685; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_1_7; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000488; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase 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; 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; 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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000313|EMBL:AEI68818.1};
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}.
FT DOMAIN 351..530
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 533..626
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 746 AA; 80064 MW; 372FCFAB78336ECD CRC64;
MATKAEELEV KQGFSYQVED GVAVITFDLP DSPVNTLSPE TGEAFLRVMS RAEREPEVKA
VVFTSGKKDS FVAGAKIDFL HTIKTAEEAT AISRNGQEGF DKLDAFPKPV VAAIHGACLG
GGLEWALACD YRVATDSPKT SLGLPEVQLG LIPGAGGTQR LPALIGVQAA LDLILTGKSL
KPGKAKKLGV VDEVVPAPIL RAIAVRRAKE LAEGKLKVER RHGQGFKGVA AGGKSKGLAG
FIQGLANKEL WAEVALEDNP LGRKVLFDQA RKQLLKKTRG KFPAPEKALQ VVRVGLESGH
KAGQEAEAKA FGELVVSDVS KRLVEIFFAT TALKKENGTA SPDAKPREVK KVAVLGGGLM
GGGIAYVASS LQGVPVRVKD KDDAGVGRAM KQVQSILDER VKRRSLTRRE ATAKSALVTA
GTDYAGFKSA DLVIEAVFED LKLKHRIIAE VEAVTGDQTI FASNTSSIPI TELAKGSRRP
AQVIGMHYFS PVHKMPLLEV ITHAGTADWV TATCVEVGRK QGKTVIVVND GPGFYTSRIL
APYMNEAAYL LAEGADIAEL DRALVEFGFP VGPMTLLDEV GIDVAQKVGP IMEAAFGKRM
AAPKALEKVV ADGRLGRKTE KGFYLYEGGK KQEVDPSIYA LLPHGTERRS FDRAEMAERV
VLQMVNEAIR CLGEGILRSA RDGDVGAIFG LGFPPFLGGP FHYVDSRGPA DVLRKLEHFH
DKLGERFVPA PHLVEMVKAG KTFYPR
//
