ID   CAIB_PROSL              Reviewed;         406 AA.
AC   Q8GB19;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=L-carnitine CoA-transferase;
DE            EC=2.8.3.21;
DE   AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase;
GN   Name=caiB;
OS   Proteus sp. (strain LE138).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=217617;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Engemann C., Elssner T., Pfeifer S., Krumbholz C., Maier T., Kleber H.-P.;
RT   "Cai locus and corresponding enzymes of Proteus sp.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-25, AND SUBUNIT.
RX   PubMed=11409545; DOI=10.1007/s002030100272;
RA   Engemann C., Elssner T., Kleber H.-P.;
RT   "Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.";
RL   Arch. Microbiol. 175:353-359(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:0000269|PubMed:11409545}.
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; AJ508908; CAD48580.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GB19; -.
DR   SMR; Q8GB19; -.
DR   KEGG; ag:CAD48580; -.
DR   BRENDA; 2.8.3.21; 5048.
DR   UniPathway; UPA00117; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Transferase.
FT   CHAIN           1..406
FT                   /note="L-carnitine CoA-transferase"
FT                   /id="PRO_0000194711"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        21
FT                   /note="S -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  45312 MW;  F979DA820E8B9AA3 CRC64;
     MTEHLPMPQF GPLAGVRVVF SGIEIAGPFA GQMFAEWGAE VIWIENVAWA DTIRVQPHYP
     QLSRRNLHAL SLNIFKDGGR DAFLKLMETT DIFIEASKGP AFARRGITDE VLWEHNPKLV
     IAHLSGFGQY GDPQYTNLPA YNTIAQAFSG YLIQNGDKDQ PMPAFPYTAD YFSGMTATTS
     ALAALYKVQQ TGKGESIDIA MYEVMLRMGQ YFMMDYFNGG EICPRMTKGK EPYYAGCGLY
     RCQDGYIVME VVGITQIEEI FKDIGLAHLL GTPEVPKGTQ LIHRINCPHG QLFEDELDEW
     LANQPITAVL KRLSELNIAS AKVLTIPELE GNPQYVARES ITQWKTMSGE TCKGPNIMPK
     FKNNPGKIWR GMPAHGMDTN AILKNIGYSD EQIRELVDKG LAKIVE