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Database: UniProt
Entry: Q668V1
LinkDB: Q668V1
Original site: Q668V1 
ID   FADJ_YERPS              Reviewed;         753 AA.
AC   Q668V1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   19-FEB-2014, entry version 71.
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=YPTB2636;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH21874.1; Type=Erroneous initiation;
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DR   EMBL; BX936398; CAH21874.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_071146.1; NC_006155.1.
DR   ProteinModelPortal; Q668V1; -.
DR   STRING; 273123.YPTB2636; -.
DR   EnsemblBacteria; CAH21874; CAH21874; YPTB2636.
DR   GeneID; 2955529; -.
DR   KEGG; yps:YPTB2636; -.
DR   PATRIC; 18644321; VBIYerPse22266_3218.
DR   eggNOG; COG1250; -.
DR   HOGENOM; HOG000261346; -.
DR   KO; K01782; -.
DR   OMA; MMLNEAA; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   ProtClustDB; PRK11154; -.
DR   BioCyc; YPSE273123:GI1M-2723-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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; SSF48179; 2.
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    753       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_0000109316.
FT   REGION        8    197       Enoyl-CoA hydratase (By similarity).
FT   REGION      313    747       3-hydroxyacyl-CoA dehydrogenase (By
FT                                similarity).
FT   SITE        125    125       Important for catalytic activity (By
FT                                similarity).
FT   SITE        147    147       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   753 AA;  81350 MW;  8E5EB7D4B900DF93 CRC64;
     MGASATNSVT HPAFTLNVRP DNIGIITIDV VGDKVNTLKA EFADQIATIL QQAHALPKLQ
     GLVIVSGKPD SFIAGADITM IAACRTAHDA RVLAQKGQSI LAQIAAFPVP VVAAIHGACL
     GGGLELALAC HSRICSLDDK TVLGLPEVQL GLLPGSGGTQ RLPRLVGVSK ALDMILTGKQ
     IRPRQALKMG LVDDVVPRDI LLDVAIQRAK AGWLNRRALP WQERLLSGPL GKALLFRIVR
     KKTLAKTRGH YPAAERIIDV VRKGLDQGGP SGYEAEARAF GELAMSPQSA ALRSLFFATT
     SLKKETGSAA TARAIHRVGV LGGGLMGGGI ANVTATRAGL PVRIKDINPQ GINQALKYTW
     DALGKRVRSK RMRPTEQQRQ MMLISGSTDY RGFERVDIVV EAVFEDLSLK QQMVADIERF
     GAAHTIFASN TSSLPISQIA ALAQRPEQVI GLHYFSPVDK MPLVEVIPHE KTSEETIATT
     VALARKQGKT AIVVADRAGF YVNRILAPYI NEAARCLLDG EPIESVDNAL VDFGFPVGPM
     MLLDEVGIDV ATKIMPILVE QLGPRFAAPP SFDVILKDGR KGRKNGRGFY LYSNPTLHSN
     STKNSSPTKN GNSPAKRNSF KWRKNKVKPV DSSIYTLLGV TPKAHLGAGV ITQRCTMLML
     NEAVRCLDES IIRNPRDGDI GAVFGIGFPP FLGGPFRYLD SLGADKVVQA LRLLVQQYGE
     RFEPCQRLVT MAEQQQQFYP VDANIDEVTD VAS
//
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