Identification
Name:Crotonobetainyl-CoA:carnitine CoA-transferase
Synonyms:Not Available
Gene Name:caiB
Enzyme Class:
Biological Properties
General Function:Involved in catalytic 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
Cellular Location:Cytoplasm
SMPDB Pathways:
  • L-carnitine degradation I PW002037
  • Operon: 16S ribosomal RNA modification & chaperone PW001877
  • Operon: probable carnitine operon PW001875
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB23848(E)-4-(Trimethylammonio)but-2-enoyl-CoAMetaboCard
ECMDB239014-Trimethylammoniobutanoyl-CoAMetaboCard
ECMDB00062CarnitineMetaboCard
ECMDB21321CrotonobetaineMetaboCard
ECMDB20539Crotonobetainyl-CoAMetaboCard
ECMDB20541D-Carnitinyl-CoAMetaboCard
ECMDB21336gamma-ButyrobetaineMetaboCard
ECMDB20559gamma-Butyrobetainyl-CoAMetaboCard
ECMDB23900L-CarnitineMetaboCard
ECMDB20578L-Carnitinyl-CoAMetaboCard
GO Classification:
Function
catalytic activity
Process
metabolic process
Gene Properties
Blattner:b0038
Gene OrientationCounterclockwise
Centisome Percentage:0.82
Left Sequence End37898
Right Sequence End39115
Gene Sequence:
>1218 bp
ATGGATCATCTACCCATGCCGAAATTCGGGCCGTTGGCCGGATTGCGCGTTGTCTTCTCC
GGTATCGAAATCGCCGGACCGTTTGCCGGGCAAATGTTCGCAGAATGGGGCGCGGAAGTT
ATCTGGATCGAGAACGTCGCCTGGGCCGACACCATTCGCGTTCAACCGAACTACCCGCAA
CTCTCCCGCCGCAATTTGCACGCGCTGTCGTTAAATATTTTCAAAGATGAAGGCCGCGAA
GCGTTTCTGAAATTAATGGAAACCACCGATATCTTCATCGAAGCCAGTAAAGGTCCGGCC
TTTGCCCGTCGTGGCATTACCGATGAAGTACTGTGGCAGCACAACCCGAAACTGGTTATC
GCTCACCTGTCCGGTTTTGGTCAGTACGGCACCGAGGAGTACACCAATCTTCCGGCCTAT
AACACTATCGCCCAGGCCTTTAGTGGTTACCTGATTCAGAACGGTGATGTTGACCAGCCA
ATGCCTGCCTTCCCGTATACCGCCGATTACTTTTCTGGCCTGACCGCCACCACGGCGGCG
CTGGCAGCACTGCATAAAGTGCGTGAAACCGGTAAAGGCGAAAGTATCGACATCGCCATG
TATGAAGTGATGCTGCGTATGGGCCAGTACTTCATGATGGATTACTTCAACGGCGGCGAA
ATGTGCCCGCGCATGAGCAAAGGTAAAGATCCCTACTACGCCGGTTGCGGTCTGTATAAA
TGTGCCGACGGCTACATCGTGATGGAACTGGTGGGCATTACCCAAATTGAAGAGTGCTTT
AAAGATATTGGCCTCGCACATCTGCTTGGCACGCCAGAAATCCCGGAAGGCACTCAGCTT
ATCCACCGTATCGAATGCCCTTACGGCCCACTGGTTGAAGAGAAACTCGATGCCTGGCTG
GCGACACATACCATCGCGGAAGTAAAAGAACGCTTTGCTGAACTGAATATCGCCTGCGCC
AAAGTGCTGACCGTACCGGAACTGGAAAGCAATCCACAGTATGTGGCTCGCGAATCAATC
ACTCAGTGGCAAACGATGGATGGTCGCACCTGCAAAGGGCCGAACATCATGCCGAAATTC
AAAAATAACCCCGGACAAATCTGGCGCGGAATGCCCTCACATGGCATGGACACGGCTGCC
ATTTTGAAAAATATCGGCTACAGCGAAAACGACATTCAGGAGTTGGTCAGCAAAGGTCTG
GCCAAAGTTGAGGACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:405
Protein Molecular Weight:45126
Protein Theoretical pI:5
PDB File:1XVV
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Crotonobetainyl-CoA:carnitine CoA-transferase
MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQ
LSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVI
AHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAA
LAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYK
CADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWL
ATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKF
KNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED
References
External Links:
ResourceLink
Uniprot ID:P31572
Uniprot Name:CAIB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321920
PDB ID:1XVV
Ecogene ID:EG11559
Ecocyc:EG11559
ColiBase:b0038
Kegg Gene:b0038
EchoBASE ID:EB1520
CCDB:CAIB_ECOLI
BacMap:16128032
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Eichler, K., Bourgis, F., Buchet, A., Kleber, H. P., Mandrand-Berthelot, M. A. (1994). "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli." Mol Microbiol 13:775-786. Pubmed: 7815937
  • Eichler, K., Schunck, W. H., Kleber, H. P., Mandrand-Berthelot, M. A. (1994). "Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase." J Bacteriol 176:2970-2975. Pubmed: 8188598
  • Elssner, T., Engemann, C., Baumgart, K., Kleber, H. P. (2001). "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 40:11140-11148. Pubmed: 11551212
  • Elssner, T., Preusser, A., Wagner, U., Kleber, H. P. (1999). "Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions." FEMS Microbiol Lett 174:295-301. Pubmed: 10339822
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Stenmark, P., Gurmu, D., Nordlund, P. (2004). "Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism." Biochemistry 43:13996-14003. Pubmed: 15518548
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901