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FADJ_ECOHS
ID   FADJ_ECOHS              Reviewed;         714 AA.
AC   A8A2L0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01617};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01617};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01617};
GN   Name=fadJ {ECO:0000255|HAMAP-Rule:MF_01617}; OrderedLocusNames=EcHS_A2492;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition of
CC       water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-
CC       hydroxyacyl-CoA dehydrogenase activities. {ECO:0000255|HAMAP-
CC       Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01617};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01617};
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:0000255|HAMAP-Rule:MF_01617};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01617};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC       (FadI). {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
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DR   EMBL; CP000802; ABV06764.1; -; Genomic_DNA.
DR   RefSeq; WP_000424985.1; NC_009800.1.
DR   AlphaFoldDB; A8A2L0; -.
DR   SMR; A8A2L0; -.
DR   KEGG; ecx:EcHS_A2492; -.
DR   HOGENOM; CLU_009834_16_1_6; -.
DR   OMA; PFRYMDT; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001123; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01617; FadJ; 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; IPR012802; FadJ.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02440; FadJ; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation;
KW   Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.
FT   CHAIN           1..714
FT                   /note="Fatty acid oxidation complex subunit alpha"
FT                   /id="PRO_1000069484"
FT   REGION          1..190
FT                   /note="Enoyl-CoA hydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   REGION          306..714
FT                   /note="3-hydroxyacyl-CoA dehydrogenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   SITE            118
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
SQ   SEQUENCE   714 AA;  77038 MW;  0CA2A6A13D419BEF CRC64;
     MEMASAFTLN VRLDNIAIIT IDVPDEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFISA
     KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA
     LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL
     KLGLVDDVVP HSILLEAAVE LAKKDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
     QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTDVKKDPG
     SDAPPAPLNS VGILGGGLMG AGIAYVTACK AGLPVRIKDI NPQGINHALK YSWDQLEGKV
     RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF
     ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ
     GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERVEHID AALVKFGFPV GPIQLLDEVG
     IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
     IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV FGIGFPPFLG
     GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMGA RGESFWKTTA TDLQ
 
 
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