ID FADJ_ECOSM Reviewed; 714 AA.
AC B1LME7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 01-MAY-2013, entry version 45.
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=EcSMS35_2500;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia
RT coli SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB18415.1; -; Genomic_DNA.
DR RefSeq; YP_001744544.1; NC_010498.1.
DR ProteinModelPortal; B1LME7; -.
DR SMR; B1LME7; 1-707.
DR STRING; 439855.EcSMS35_2500; -.
DR EnsemblBacteria; ACB18415; ACB18415; EcSMS35_2500.
DR GeneID; 6146373; -.
DR KEGG; ecm:EcSMS35_2500; -.
DR PATRIC; 18433898; VBIEscCol6161_2665.
DR eggNOG; COG1250; -.
DR HOGENOM; HOG000261346; -.
DR KO; K01782; -.
DR OMA; SPKRDKG; -.
DR ProtClustDB; PRK11154; -.
DR BioCyc; ECOL439855:GHHB-2989-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; 2.
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_1000185944.
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; 77074 MW; 3B3600CF8971C888 CRC64;
MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA
KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL PVPVIAAIHG ACLGGGLELA
LACHGRVCTD DAKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL
KLGLVDDVVP QSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDSG
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLSVRIKDI NPQGINHALK YSWDQLEGKV
RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL ELKQQMVAEV EQNCATHTIF
ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHASTSAQTI ATTVKLAKKQ
GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERIEHID AALVKFGFPV GPIQLLDEVG
IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV FGIGFPPFLG
GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMSK RGESFWKTTA TDLQ
//
