ID   CAIA_SALSV              Reviewed;         380 AA.
AC   B4TWR6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=SeSA_A0081;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001127; ACF92959.1; -; Genomic_DNA.
DR   RefSeq; WP_000347134.1; NC_011094.1.
DR   AlphaFoldDB; B4TWR6; -.
DR   SMR; B4TWR6; -.
DR   EnsemblBacteria; ACF92959; ACF92959; SeSA_A0081.
DR   KEGG; sew:SeSA_A0081; -.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   OMA; CFITNSG; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001865; 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_1000136285"
SQ   SEQUENCE   380 AA;  42481 MW;  4A7A39798EDFC806 CRC64;
     MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSVYPE RFVKALADMG IDSLLIPEEH
     GGLEAGFVTV AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW
     NSAITEPGAG SDVGSLKTTY TRKNGKVYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY
     TEWFVDMSKA GIKVNKLEKL GLRMDSCCEI TFDDVELDEK DMFGREGNGF NRVKEEFDHE
     RFLVALTNYG TAMCAFEDAA RYANQRVQFG EAIGRFQLIQ EKFAHMAIKL NSMKNMLLEA
     AWKADNGTIT SGDAAMCKYF CANAAFEVVD TAMQVLGGVG IAGNHRITRF WRDLRVDRVS
     GGSDEMQILT LGRAVLKQYR