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Database: UniProt
Entry: A4TM82
LinkDB: A4TM82
Original site: A4TM82 
ID   FADJ_YERPP              Reviewed;         774 AA.
AC   A4TM82;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   29-OCT-2014, entry version 61.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01617};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01617};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01617};
GN   Name=fadJ {ECO:0000255|HAMAP-Rule:MF_01617};
GN   OrderedLocusNames=YPDSF_2013;
OS   Yersinia pestis (strain Pestoides F).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=386656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pestoides F;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Worsham P., Chu M.,
RA   Bearden S., Garcia E., Richardson P.;
RT   "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta
CC       chains (FadI). {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CC       CoA dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
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DR   EMBL; CP000668; ABP40394.1; -; Genomic_DNA.
DR   RefSeq; YP_001163367.1; NC_009381.1.
DR   ProteinModelPortal; A4TM82; -.
DR   STRING; 386656.YPDSF_2013; -.
DR   EnsemblBacteria; ABP40394; ABP40394; YPDSF_2013.
DR   GeneID; 5065641; -.
DR   KEGG; ypp:YPDSF_2013; -.
DR   PATRIC; 18613436; VBIYerPes122972_2620.
DR   eggNOG; COG1250; -.
DR   HOGENOM; HOG000261346; -.
DR   KO; K01782; -.
DR   OMA; PFRYMDT; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   BioCyc; YPES386656:GKD7-2049-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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   Gene3D; 3.90.226.10; -; 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; IPR029045; ClpP/crotonase-like_dom.
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   SUPFAM; SSF52096; SSF52096; 1.
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    774       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_0000323533.
FT   REGION        1    224       Enoyl-CoA hydratase. {ECO:0000255|HAMAP-
FT                                Rule:MF_01617}.
FT   REGION      340    774       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01617}.
FT   SITE        152    152       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01617}.
FT   SITE        174    174       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01617}.
SQ   SEQUENCE   774 AA;  83594 MW;  D10D346111BFD403 CRC64;
     MSKENIVTRE NTAVSENAVS EPTVNNDVGA SATNSVTHPA FTLNVRPDNI GIITIDVVGD
     KVNTLKAEFA DQIATILQQA HALPKLQGLV IVSGKPDSFI AGADITMIAA CRTAHDARVL
     AQKGQSILAQ IAAFPVPVVA AIHGACLGGG LELALACHSR ICSLDDKTVL GLPEVQLGLL
     PGSGGTQRLP RLVGVSKALD MILTGKQIRP RQALKMGLVD DVVPRDILLD VAIQRAKAGW
     LNRRALPWQE RLLSGPLGKA LLFRIVRKKT LAKTRGHYPA AERIIDVVRK GLDQGGPSGY
     EAEARAFGEL AMSPQSAALR SLFFATTSLK KETGSAATAR AIHRVGVLGG GLMGGGIANV
     TATRAGLPVR IKDINPQGIN QALKYTWDAL GKRVRSKRMR PTEQQRQMML ISGSTDYRGF
     ERVDIVVEAV FEDLSLKQQM VADIERFGAA HTIFASNTSS LPISQIAALA QRPEQVIGLH
     YFSPVDKMPL VEVIPHEKTS EETIATTVAL ARKQGKTAIV VADRAGFYVN RILAPYINEA
     ARCLLDGEPI ESVDNALVDF GFPVGPMMLL DEVGIDVATK IMPILVEQLG PRFAAPPSFD
     VILKDGRKGR KNGRGFYLYS NPTKNSSPTK NGNSPAKRNS FKWRKNKVKP VDASIYTLLG
     VTPKAHLGAG VITQRCTMLM LNEAVRCLDE SIIRNPRDGD IGAVFGIGFP PFLGGPFRYL
     DSLGADKVVQ ALRLLVQQYG ERFEPCQRLV TMAEQQQQFY PVDANIDEVT DVAS
//
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