ID   CAIA_SALAR              Reviewed;         380 AA.
AC   A9MQH5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 103.
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};
GN   OrderedLocusNames=SARI_02927;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of crotonobetainyl-CoA to gamma-
CC       butyrobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(trimethylamino)butanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] + H(+) = crotonobetainyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:51584, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000880; ABX22773.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MQH5; -.
DR   SMR; A9MQH5; -.
DR   STRING; 41514.SARI_02927; -.
DR   KEGG; ses:SARI_02927; -.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000002084; 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:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00567; ACAD; 1.
DR   FunFam; 1.20.140.10:FF:000001; Acyl-CoA dehydrogenase; 1.
DR   FunFam; 2.40.110.10:FF:000002; Acyl-CoA dehydrogenase fadE12; 1.
DR   FunFam; 1.10.540.10:FF:000005; Crotonobetainyl-CoA reductase; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   HAMAP; MF_01052; CaiA; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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; IPR006091; AcylCoA_DH/ox_M.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR023450; CaiA.
DR   NCBIfam; NF002885; PRK03354.1; 1.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
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   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Crotonobetainyl-CoA reductase"
FT                   /id="PRO_1000084429"
SQ   SEQUENCE   380 AA;  42533 MW;  FEE1E446A19D7251 CRC64;
     MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSIYPE RFVKALAEMG IDSLLIPEEH
     GGLDAGFVTV AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW
     NSAITEPGAG SDVGSLKTTY TRKNGKVYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY
     TEWFVDMSKP GIKVTKLEKL GLRMDSCCEI TFDEVELDEK DRFGREGNGF NRVKEEFDHE
     RFLVALTNYG TAMCAFEDAA RYANQRVQFG ETIGRFQLIQ EKFAHMAIKL NAMKNMLLEA
     AWKADNGTIT SGDAAMCKYF CANAAFEVVD SAMQVLGGVG IAGNHRISRF WRDLRVDRVS
     GGSDEMQILT LGRAVLKQYR
//