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-MAY-2013, entry version 39.
DE RecName: Full=Crotonobetainyl-CoA dehydrogenase;
DE EC=1.3.99.-;
DE AltName: Full=Crotonobetainyl-CoA reductase;
GN Name=caiA; 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 (By similarity).
CC -!- COFACTOR: FAD (By similarity).
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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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; YSAAIVW; -.
DR ProtClustDB; PRK03354; -.
DR BioCyc; ECOL331112:GHHI-200-MONOMER; -.
DR UniPathway; UPA00117; -.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:HAMAP.
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; IPR006092; Acyl-CoA_DH_N.
DR InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
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.
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; SSF56645; AcylCoA_dehyd_NM; 1.
DR SUPFAM; SSF47203; AcylCoADH_C_like; 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
//