(data stored in ACNUC7421 zone)

SWISSPROT: CAIB_ECO27

ID   CAIB_ECO27              Reviewed;         405 AA.
AC   B7UI84;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
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};
GN   OrderedLocusNames=E2348C_0039;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the CoA moiety from
CC       gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-
CC       CoA and gamma-butyrobetaine. Is also able to catalyze the
CC       reversible transfer of the CoA moiety from gamma-butyrobetainyl-
CC       CoA or L-carnitinyl-CoA to crotonobetaine to generate
CC       crotonobetainyl-CoA. {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;
CC         EC=2.8.3.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01050};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + gamma-butyrobetainyl-CoA = (R)-
CC         carnitinyl-CoA + 4-(trimethylamino)butanoate;
CC         Xref=Rhea:RHEA:28418, ChEBI:CHEBI:16244, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:60932, ChEBI:CHEBI:61513; EC=2.8.3.21;
CC         Evidence={ECO:0000255|HAMAP-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 CaiB/BaiF CoA-transferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01050}.
DR   EMBL; FM180568; CAS07587.1; -; Genomic_DNA.
DR   RefSeq; WP_000349968.1; NC_011601.1.
DR   SMR; B7UI84; -.
DR   EnsemblBacteria; CAS07587; CAS07587; E2348C_0039.
DR   KEGG; ecg:E2348C_0039; -.
DR   KO; K08298; -.
DR   OMA; RPGQHND; -.
DR   BioCyc; ECOL574521:E2348C_RS00205-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008205; 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; 3.40.50.10540; -; 1.
DR   HAMAP; MF_01050; CaiB; 1.
DR   InterPro; IPR023452; CoA-Trfase_CaiB.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UI84.
DR   SWISS-2DPAGE; B7UI84.
KW   Complete proteome; Cytoplasm; Transferase.
FT   CHAIN         1    405       L-carnitine CoA-transferase.
FT                                /FTId=PRO_1000149622.
FT   ACT_SITE    169    169       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01050}.
FT   BINDING      97     97       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01050}.
FT   BINDING     104    104       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01050}.
SQ   SEQUENCE   405 AA;  45057 MW;  1908CC7F264ACAD5 CRC64;
     MDHLTMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
     LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
     AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
     LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMTKGKD PYYAGCGLYK
     CADGYIVMEL VGITQIAECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
     AAHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
//

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