ID FADJ_YERE8 Reviewed; 745 AA.
AC A1JK30;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 01-MAY-2013, entry version 52.
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; Synonyms=faoA; OrderedLocusNames=YE1277;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the
RT high pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL11369.1; Type=Erroneous initiation;
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DR EMBL; AM286415; CAL11369.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_001005598.1; NC_008800.1.
DR ProteinModelPortal; A1JK30; -.
DR STRING; 393305.YE1277; -.
DR GeneID; 4715636; -.
DR KEGG; yen:YE1277; -.
DR PATRIC; 18562028; VBIYerEnt11519_1387.
DR eggNOG; COG1250; -.
DR HOGENOM; HOG000261346; -.
DR KO; K01782; -.
DR ProtClustDB; PRK11154; -.
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 1 745 Fatty acid oxidation complex subunit
FT alpha.
FT /FTId=PRO_0000323532.
FT REGION 47 209 Enoyl-CoA hydratase (By similarity).
FT REGION 325 745 3-hydroxyacyl-CoA dehydrogenase (By
FT similarity).
FT SITE 137 137 Important for catalytic activity (By
FT similarity).
FT SITE 159 159 Important for catalytic activity (By
FT similarity).
SQ SEQUENCE 745 AA; 79924 MW; B31E7B68E3F51798 CRC64;
MSQENTLNSG DETILAEAVA PAHAVFTLSV RPDNIGIITV DVVGDKVNTL KAKFAEQIAE
ILQQAQALSQ LQGLVIISGK PDSFIAGADI TMIAACHTAQ DARILAQKGQ SILAQIAAFP
VPVVAAIHGA CLGGGLELAL ACHSRICSQD DKTVLGLPEV QLGLLPGSGG TQRLPRLVGV
SKALDMILTG RQVRARQALK MGLVDDVVPQ DILLDVAIQR AKAGWLDKPA LPWQERLLSG
PLGKALLFNI VRKKTQAKTK GHYPAAERII DVVRKGLDHG GPAGYEAEAK AFGELAMTPE
SAALRSLFFA TTSLKKESGG KAQPRAIHRV GVLGGGLMGG GIANVTATRA GLPVRIKDIN
PTGINQALKY TWDTLGKRVR SKRMRPAERQ RQMMLISGST DYCGFGNVDI VVEAVFEDLS
LKQQMVADIE HFAAPHTIFA SNTSSLPISD IAAQAQRPEQ VIGLHYFSPV DKMPLVEVIP
HAKTSEETIA TTVALARKQG KTAIVVADRA GFYVNRILAP YINEAARCLL DGEPIASVDK
ALVDFGFPVG PITLLDEVGI DVGTKIIPIL VEKLGARFAA PPSFDVILKD GRKGRKNGRG
FYLYPAKSSG FKWKRSPVKQ VDTSVYTLLG VTPKAHLESA VIAQRCTMMM LNEAARCLDE
SIIRNPRDGD IGAVFGIGFP PFLGGPFRYM DSLGADKVVK TLNLLAQQYG ERFEPCSLLV
TMAGQQKRFY PPENSLDEAA ITAHN
//
