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 01-MAY-2013, entry version 57.
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].
RC STRAIN=536 / UPEC;
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 a hydroxyacyl-CoA by addition
CC of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase
CC and 3-hydroxyacyl-CoA dehydrogenase activities (By 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; NC_008253.1.
DR ProteinModelPortal; Q0TFA6; -.
DR SMR; Q0TFA6; 1-707.
DR STRING; 362663.ECP_2379; -.
DR EnsemblBacteria; ABG70373; ABG70373; ECP_2379.
DR GeneID; 4188711; -.
DR KEGG; ecp:ECP_2379; -.
DR PATRIC; 18195537; VBIEscCol77757_2412.
DR eggNOG; COG1250; -.
DR HOGENOM; HOG000261346; -.
DR KO; K01782; -.
DR OMA; SPKRDKG; -.
DR PhylomeDB; Q0TFA6; -.
DR ProtClustDB; PRK11154; -.
DR BioCyc; ECOL362663:GIY5-2391-MONOMER; -.
DR UniPathway; UPA00659; -.
DR GO; GO:0016507; C:mitochondrial 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 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 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; IPR001753; Crotonase_core_superfam.
DR InterPro; IPR013328; DH_multihelical.
DR InterPro; IPR012802; FadJ.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH; 1.
DR SUPFAM; SSF48179; 6DGDH_C_like; 2.
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 SITE 118 118 Important for catalytic activity (By
FT similarity).
FT SITE 140 140 Important for catalytic activity (By
FT 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
//
