ID   CAIB_SALTI              Reviewed;         405 AA.
AC   Q8Z9L3;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=STY0082, t0073;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL513382; CAD01226.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO67806.1; -; Genomic_DNA.
DR   RefSeq; NP_454682.1; NC_003198.1.
DR   RefSeq; WP_001016209.1; NZ_WSUR01000028.1.
DR   AlphaFoldDB; Q8Z9L3; -.
DR   SMR; Q8Z9L3; -.
DR   STRING; 220341.16501355; -.
DR   EnsemblBacteria; AAO67806; AAO67806; t0073.
DR   KEGG; stt:t0073; -.
DR   KEGG; sty:STY0082; -.
DR   PATRIC; fig|220341.7.peg.81; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_2_0_6; -.
DR   OMA; HRPGFGT; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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; Transferase.
FT   CHAIN           1..405
FT                   /note="L-carnitine CoA-transferase"
FT                   /id="PRO_0000194712"
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;  44866 MW;  A1E68840E512500D 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
     AAHTIADVQA RFAELNIACA KVLTIPELEG NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGKIWRG MPSHGMDTAA ILKNIGYSEA DIKELVGKGL AKVED