CAIB_SALCH
ID CAIB_SALCH Reviewed; 405 AA.
AC Q57TI9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=L-carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
DE EC=2.8.3.21 {ECO:0000255|HAMAP-Rule:MF_01050};
DE AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
GN Name=caiB {ECO:0000255|HAMAP-Rule:MF_01050}; OrderedLocusNames=SCH_0066;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01050}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01050};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01050};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01050}.
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DR EMBL; AE017220; AAX63972.1; -; Genomic_DNA.
DR RefSeq; WP_001016212.1; NC_006905.1.
DR AlphaFoldDB; Q57TI9; -.
DR SMR; Q57TI9; -.
DR EnsemblBacteria; AAX63972; AAX63972; SCH_0066.
DR KEGG; sec:SCH_0066; -.
DR HOGENOM; CLU_033975_2_0_6; -.
DR OMA; HRPGFGT; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000538; 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_0000300981"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT BINDING 97
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT BINDING 104
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
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