(data stored in ACNUC7421 zone)

SWISSPROT: CAIB_ECODH

ID   CAIB_ECODH              Reviewed;         405 AA.
AC   B1XBG3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 57.
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=ECDH10B_0039;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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: (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-
CC       carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-
CC       CoA. {ECO:0000255|HAMAP-Rule:MF_01050}.
CC   -!- CATALYTIC ACTIVITY: 4-trimethylammoniobutanoyl-CoA + L-carnitine =
CC       4-trimethylammoniobutanoate + L-carnitinyl-CoA.
CC       {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; CP000948; ACB01243.1; -; Genomic_DNA.
DR   RefSeq; WP_000349936.1; NC_010473.1.
DR   ProteinModelPortal; B1XBG3; -.
DR   SMR; B1XBG3; -.
DR   EnsemblBacteria; ACB01243; ACB01243; ECDH10B_0039.
DR   KEGG; ecd:ECDH10B_0039; -.
DR   eggNOG; ENOG4105C04; Bacteria.
DR   eggNOG; COG1804; LUCA.
DR   HOGENOM; HOG000219745; -.
DR   KO; K08298; -.
DR   OMA; SGFRYIN; -.
DR   UniPathway; UPA00117; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-containing groups; IEA:InterPro.
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.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XBG3.
DR   SWISS-2DPAGE; B1XBG3.
KW   Cytoplasm; Transferase.
FT   CHAIN         1    405       L-carnitine CoA-transferase.
FT                                /FTId=PRO_1000136249.
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;  45127 MW;  75583684B4B5A2DE CRC64;
     MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
     LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
     AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
     LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK
     CADGYIVMEL VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
     ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
//

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