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Database: UniProt
Entry: B1IXA5
LinkDB: B1IXA5
Original site: B1IXA5 
ID   FADJ_ECOLC              Reviewed;         714 AA.
AC   B1IXA5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   29-OCT-2014, entry version 52.
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};
GN   OrderedLocusNames=EcolC_1312;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition
CC       of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase
CC       and 3-hydroxyacyl-CoA dehydrogenase activities.
CC       {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA. {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
CC       chains (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-
CC       CoA dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
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DR   EMBL; CP000946; ACA76978.1; -; Genomic_DNA.
DR   RefSeq; YP_001724305.1; NC_010468.1.
DR   ProteinModelPortal; B1IXA5; -.
DR   SMR; B1IXA5; 1-707.
DR   STRING; 481805.EcolC_1312; -.
DR   EnsemblBacteria; ACA76978; ACA76978; EcolC_1312.
DR   GeneID; 6068474; -.
DR   KEGG; ecl:EcolC_1312; -.
DR   PATRIC; 18225337; VBIEscCol82905_1403.
DR   eggNOG; COG1250; -.
DR   HOGENOM; HOG000261346; -.
DR   KO; K01782; -.
DR   OMA; PFRYMDT; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   BioCyc; ECOL481805:GI3G-1350-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 2.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.226.10; -; 1.
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_C-like.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR012802; FadJ.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02440; FadJ; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    714       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000088061.
FT   REGION        1    190       Enoyl-CoA hydratase. {ECO:0000255|HAMAP-
FT                                Rule:MF_01617}.
FT   REGION      306    714       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01617}.
FT   SITE        118    118       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01617}.
FT   SITE        140    140       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01617}.
SQ   SEQUENCE   714 AA;  77169 MW;  79B8B735A866DEC8 CRC64;
     MEMASAFTLN VRLDNIAIIT IDVPDEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFISA
     KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA
     LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL
     KLGLVDDVVP HSILLEAAVE LVKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
     QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTDVKKDPG
     SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPQGINHALK YSWDQLEGKV
     RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF
     ASNTSSLPIG DIAAHATRPE 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 PCERLVEMSK RGESFWKTTA TDLQ
//
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