ID   CAIA_ECOL6              Reviewed;         380 AA.
AC   P60585; P31571;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Crotonobetainyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_01052};
DE            EC=1.3.8.13 {ECO:0000255|HAMAP-Rule:MF_01052};
DE   AltName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01052};
GN   Name=caiA {ECO:0000255|HAMAP-Rule:MF_01052}; OrderedLocusNames=c0048;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reduction of crotonobetainyl-CoA to gamma-
CC       butyrobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-butyrobetainyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = crotonobetainyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:51584, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:60933, ChEBI:CHEBI:61513; EC=1.3.8.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01052};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={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   -!- SUBCELLULAR LOCATION: Cytoplasm {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; AE014075; AAN78546.1; -; Genomic_DNA.
DR   RefSeq; WP_000347117.1; NC_004431.1.
DR   AlphaFoldDB; P60585; -.
DR   SMR; P60585; -.
DR   STRING; 199310.c0048; -.
DR   EnsemblBacteria; AAN78546; AAN78546; c0048.
DR   GeneID; 67416114; -.
DR   KEGG; ecc:c0048; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   OMA; CFITNSG; -.
DR   BioCyc; ECOL199310:C0048-MON; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
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_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR023450; 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   Cytoplasm; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..380
FT                   /note="Crotonobetainyl-CoA reductase"
FT                   /id="PRO_0000201194"
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