ID   FADJ_ECOUT              Reviewed;         714 AA.
AC   Q1R972;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=UTI89_C2625;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE08092.1; -; Genomic_DNA.
DR   RefSeq; YP_541623.1; -.
DR   GeneID; 3991795; -.
DR   GenomeReviews; CP000243_GR; UTI89_C2625.
DR   KEGG; eci:UTI89_C2625; -.
DR   HOGENOM; Q1R972; -.
DR   OMA; Q1R972; AYAMTIP.
DR   BioCyc; ECOL364106:UTI89_C2625-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; 2.
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_0000273982.
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;  77148 MW;  D05212AF62C80111 CRC64;
     MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQIRENK ELRGVVFVSA
     KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA
     LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAV
     KLGLVDDVVP HSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
     QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTDVKKDPG
     SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPRGINHALK YSWDQLEGKV
     RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL ELKQQMVAEV EQNCATHTIF
     ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHASTSAQTI ATTVKLAKKQ
     GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERIEHID AALVKFGFPV GPIQLLDEVG
     IDTGTKIMPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
     IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV FGIGFPPFLG
     GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCDRLVEMSE RGESFWKTTA TDLQ
//