ID   CAIB_SALTY              Reviewed;         405 AA.
AC   Q8ZRX3;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=L-carnitine CoA-transferase;
DE            EC=2.8.3.21;
DE   AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase;
GN   Name=caiB; OrderedLocusNames=STM0072;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the CoA moiety from
CC       gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA
CC       and gamma-butyrobetaine. Is also able to catalyze the reversible
CC       transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-
CC       carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + crotonobetainyl-CoA = (R)-carnitinyl-CoA +
CC         crotonobetaine; Xref=Rhea:RHEA:28526, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:17237, ChEBI:CHEBI:60932, ChEBI:CHEBI:60933; EC=2.8.3.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + gamma-butyrobetainyl-CoA = (R)-carnitinyl-CoA
CC         + 4-(trimethylamino)butanoate; Xref=Rhea:RHEA:28418,
CC         ChEBI:CHEBI:16244, ChEBI:CHEBI:16347, ChEBI:CHEBI:60932,
CC         ChEBI:CHEBI:61513; EC=2.8.3.21;
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01050}.
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DR   EMBL; AE006468; AAL19036.1; -; Genomic_DNA.
DR   RefSeq; NP_459077.1; NC_003197.2.
DR   RefSeq; WP_001016212.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRX3; -.
DR   SMR; Q8ZRX3; -.
DR   STRING; 99287.STM0072; -.
DR   PaxDb; Q8ZRX3; -.
DR   EnsemblBacteria; AAL19036; AAL19036; STM0072.
DR   GeneID; 1251590; -.
DR   KEGG; stm:STM0072; -.
DR   PATRIC; fig|99287.12.peg.74; -.
DR   HOGENOM; CLU_033975_2_0_6; -.
DR   OMA; HRPGFGT; -.
DR   PhylomeDB; Q8ZRX3; -.
DR   BioCyc; SENT99287:STM0072-MON; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008410; F:CoA-transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   HAMAP; MF_01050; CaiB; 1.
DR   InterPro; IPR023452; CoA-Trfase_CaiB.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..405
FT                   /note="L-carnitine CoA-transferase"
FT                   /id="PRO_0000194713"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44896 MW;  40E68840E5034110 CRC64;
     MNHLPMPTFG PLAGVRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
     LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWEHNPKLVI
     AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGMTATTAA
     LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE ICPRMTKGKD PYYAGCGLYK
     CADGYIVMEL VGITQINECF KDIGLAHILG TPEVPEGTQL IHRVECPYGP LVEEKLDAWL
     ATHTIADVQA RFAELNIACA KVLTIPELEG NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGKIWRG MPSHGMDTAA ILKNIGYSEA DIKELVGKGL AKVED