ID   FADJ_ECOL5              Reviewed;         714 AA.
AC   Q0TFA6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase;
DE              EC=4.2.1.17;
DE              EC=5.1.2.3;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
GN   Name=fadJ; OrderedLocusNames=ECP_2379;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Catalyzes the formation of an hydroxyacyl-CoA by
CC       addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA
CC       epimerase and 3-hydroxyacyl-CoA dehydrogenase activities (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (fadJ) and two beta
CC       chains (fadI) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CC       CoA dehydrogenase family.
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DR   EMBL; CP000247; ABG70373.1; -; Genomic_DNA.
DR   RefSeq; YP_670274.1; -.
DR   GeneID; 4188711; -.
DR   GenomeReviews; CP000247_GR; ECP_2379.
DR   KEGG; ecp:ECP_2379; -.
DR   HOGENOM; Q0TFA6; -.
DR   OMA; Q0TFA6; AYAMTIP.
DR   BioCyc; ECOL362663:ECP_2379-MON; -.
DR   GO; GO:0016507; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:HAMAP.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01617; -; 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; IPR001753; Crotonase_core.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR012802; FadJ.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 2.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   TIGRFAMs; TIGR02440; FadJ; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; FALSE_NEG.
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_0000273983.
FT   REGION        1    190       Enoyl-CoA hydratase (By similarity).
FT   REGION      306    714       3-hydroxyacyl-CoA dehydrogenase (By
FT                                similarity).
FT   ACT_SITE    118    118       By similarity.
FT   ACT_SITE    140    140       Proton donor (By similarity).
SQ   SEQUENCE   714 AA;  77144 MW;  F1A53A6CAF6CEE26 CRC64;
     MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA
     KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA
     LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAV
     KLGLVDDVVP HSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
     QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDPG
     SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPQGINHALK YSWDQLEGKV
     RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL ELKQQMVAEV EQNCATHTIF
     ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHASTSAQTI ATTVKLAKKQ
     GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERIEHID TALVKFGFPV GPIQLLDEVG
     IDTGTKIMPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
     IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VCCLDEQVIR SVRDGDIGAV FGIGFPPFLG
     GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCNRFVEMSE RGESFWKTTA TDLQ
//