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Database: UniProt
Entry: A7ZVY9
LinkDB: A7ZVY9
Original site: A7ZVY9 
ID   CAIA_ECOHS              Reviewed;         380 AA.
AC   A7ZVY9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   01-OCT-2014, entry version 46.
DE   RecName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01052};
DE            EC=1.3.99.- {ECO:0000255|HAMAP-Rule:MF_01052};
DE   AltName: Full=Crotonobetainyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_01052};
GN   Name=caiA {ECO:0000255|HAMAP-Rule:MF_01052};
GN   OrderedLocusNames=EcHS_A0043;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Catalyzes the reduction of crotonobetainyl-CoA to gamma-
CC       butyrobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- COFACTOR: FAD. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01052}.
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DR   EMBL; CP000802; ABV04443.1; -; Genomic_DNA.
DR   RefSeq; YP_001456826.1; NC_009800.1.
DR   ProteinModelPortal; A7ZVY9; -.
DR   SMR; A7ZVY9; 5-377.
DR   STRING; 331112.EcHS_A0043; -.
DR   EnsemblBacteria; ABV04443; ABV04443; EcHS_A0043.
DR   GeneID; 5591853; -.
DR   KEGG; ecx:EcHS_A0043; -.
DR   PATRIC; 18310077; VBIEscCol77814_0042.
DR   eggNOG; COG1960; -.
DR   HOGENOM; HOG000131659; -.
DR   KO; K08297; -.
DR   OMA; KNMTTFL; -.
DR   OrthoDB; EOG6J48HZ; -.
DR   BioCyc; ECOL331112:GHHI-42-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   HAMAP; MF_01052; CaiA; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR023450; Crotonobetainyl-CoA_DHase_CaiA.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN         1    380       Crotonobetainyl-CoA dehydrogenase.
FT                                /FTId=PRO_1000064346.
SQ   SEQUENCE   380 AA;  42558 MW;  7076984D735652C3 CRC64;
     MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSVYPE RFVKALADMG IDSLLIPEEH
     GGLDAGFVTL AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW
     NSAITEPGAG SDVGSLKTTY TRRNGKIYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY
     TEWFVDMSKP GIKVTKLEKL GLRMDSCCEI TFDDVELDEK DMFGREGNGF NRVKEEFDHE
     RFLVALTNYG TAMCAFEDAA RYANQRVQFG EAIGRFQLIQ EKFAHMAIKL NSMKNMLYEA
     AWKADNGTIT SGDAAMCKYF CANAAFEVVD SAMQVLGGVG IAGNHRISRF WRDLRVDRVS
     GGSDEMQILT LGRAVLKQYR
//
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