L-carnitine CoA-transferase

Details

Name
L-carnitine CoA-transferase
Synonyms
  • 2.8.3.21
  • Crotonobetainyl-CoA:carnitine CoA-transferase
  • yaaN
Gene Name
caiB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020551|L-carnitine CoA-transferase
MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQ
LSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVI
AHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAA
LAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYK
CADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWL
ATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKF
KNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED
Number of residues
405
Molecular Weight
45126.41
Theoretical pI
4.89
GO Classification
Functions
carnitine dehydratase activity / CoA-transferase activity
Processes
carnitine catabolic process
Components
cytoplasm
General Function
Coa-transferase activity
Specific Function
Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0020552|L-carnitine CoA-transferase (caiB)
ATGGATCATCTACCCATGCCGAAATTCGGGCCGTTGGCCGGATTGCGCGTTGTCTTCTCC
GGTATCGAAATCGCCGGACCGTTTGCCGGGCAAATGTTCGCAGAATGGGGCGCGGAAGTT
ATCTGGATCGAGAACGTCGCCTGGGCCGACACCATTCGCGTTCAACCGAACTACCCGCAA
CTCTCCCGCCGCAATTTGCACGCGCTGTCGTTAAATATTTTCAAAGATGAAGGCCGCGAA
GCGTTTCTGAAATTAATGGAAACCACCGATATCTTCATCGAAGCCAGTAAAGGTCCGGCC
TTTGCCCGTCGTGGCATTACCGATGAAGTACTGTGGCAGCACAACCCGAAACTGGTTATC
GCTCACCTGTCCGGTTTTGGTCAGTACGGCACCGAGGAGTACACCAATCTTCCGGCCTAT
AACACTATCGCCCAGGCCTTTAGTGGTTACCTGATTCAGAACGGTGATGTTGACCAGCCA
ATGCCTGCCTTCCCGTATACCGCCGATTACTTTTCTGGCCTGACCGCCACCACGGCGGCG
CTGGCAGCACTGCATAAAGTGCGTGAAACCGGTAAAGGCGAAAGTATCGACATCGCCATG
TATGAAGTGATGCTGCGTATGGGCCAGTACTTCATGATGGATTACTTCAACGGCGGCGAA
ATGTGCCCGCGCATGAGCAAAGGTAAAGATCCCTACTACGCCGGTTGCGGTCTGTATAAA
TGTGCCGACGGCTACATCGTGATGGAACTGGTGGGCATTACCCAAATTGAAGAGTGCTTT
AAAGATATTGGCCTCGCACATCTGCTTGGCACGCCAGAAATCCCGGAAGGCACTCAGCTT
ATCCACCGTATCGAATGCCCTTACGGCCCACTGGTTGAAGAGAAACTCGATGCCTGGCTG
GCGACACATACCATCGCGGAAGTAAAAGAACGCTTTGCTGAACTGAATATCGCCTGCGCC
AAAGTGCTGACCGTACCGGAACTGGAAAGCAATCCACAGTATGTGGCTCGCGAATCAATC
ACTCAGTGGCAAACGATGGATGGTCGCACCTGCAAAGGGCCGAACATCATGCCGAAATTC
AAAAATAACCCCGGACAAATCTGGCGCGGAATGCCCTCACATGGCATGGACACGGCTGCC
ATTTTGAAAAATATCGGCTACAGCGAAAACGACATTCAGGAGTTGGTCAGCAAAGGTCTG
GCCAAAGTTGAGGACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP31572
UniProtKB Entry NameCAIB_ECOLI
GenBank Protein ID495242
GenBank Gene IDX67748
General References
  1. Eichler K, Schunck WH, Kleber HP, Mandrand-Berthelot MA: Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase. J Bacteriol. 1994 May;176(10):2970-5. [Article]
  2. Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA: Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol Microbiol. 1994 Sep;13(5):775-86. [Article]
  3. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Elssner T, Engemann C, Baumgart K, Kleber HP: Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry. 2001 Sep 18;40(37):11140-8. [Article]
  7. Elssner T, Preusser A, Wagner U, Kleber HP: Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions. FEMS Microbiol Lett. 1999 May 15;174(2):295-301. [Article]
  8. Stenmark P, Gurmu D, Nordlund P: Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism. Biochemistry. 2004 Nov 9;43(44):13996-4003. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails
DB02516(R)-carnitinyl-CoA betaineexperimentalunknownDetails