ID FADJ_SHIDS Reviewed; 714 AA.
AC Q32DJ4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 29-MAY-2013, entry version 61.
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=SDY_2542;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62611.1; -; Genomic_DNA.
DR RefSeq; YP_404102.1; NC_007606.1.
DR ProteinModelPortal; Q32DJ4; -.
DR STRING; 300267.SDY_2542; -.
DR EnsemblBacteria; ABB62611; ABB62611; SDY_2542.
DR GeneID; 3797643; -.
DR KEGG; sdy:SDY_2542; -.
DR PATRIC; 18695274; VBIShiDys99784_3060.
DR eggNOG; COG1250; -.
DR HOGENOM; HOG000261346; -.
DR KO; K01782; -.
DR OMA; SPKRDKG; -.
DR ProtClustDB; PRK11154; -.
DR BioCyc; SDYS300267:GJEW-2538-MONOMER; -.
DR UniPathway; UPA00659; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Reference proteome.
FT CHAIN 1 714 Fatty acid oxidation complex subunit
FT alpha.
FT /FTId=PRO_0000273988.
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; 77184 MW; 252F4E52F3133CA7 CRC64;
MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA
KPDNFIAGAD INMIGNCKTA QEAEALARQD QQLMAEIHAL PIPVIAAIHG ACLGGGLELA
LACHGRVCTD DPKTVLSLPE VQLGLLPGSD GTQRLPRLIG VSTALEMILT GKQLRAKQAL
KLGLVDDVVP HSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELVMTP QSQALRSIFF ASTEVKKDPG
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPQGINHALK YSWDQLEGKV
RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF
ASNTSSLPIG DIAAHATRPE QVIGLHFFSP VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ
GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERVEHID AALVKFGFPV GPIQLLDEVG
IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV FGIGFPPFLG
GPFRYIDSLG AGEVIAIMQR LATQYGSRFT PCERLVEMGA RGESFWKTTA TDLQ
//
