ECMDB: Probable crotonobetaine/carnitine-CoA ligase (P31552)

Identification

Name:

Probable crotonobetaine/carnitine-CoA ligase

Synonyms:

Not Available

Gene Name:

caiC

Enzyme Class:

Not Available

Biological Properties

General Function:

Involved in catalytic activity

Specific Function:

Could catalyze the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle

Cellular Location:

Not Available

SMPDB Pathways:

L-carnitine degradation I PW002037
Operon: 16S ribosomal RNA modification & chaperone PW001877
Operon: probable carnitine operon PW001875

KEGG Pathways:

Not Available

SMPDB Reactions:

1.0

→

1.0

1.0L-Carnitine + 1.0Coenzyme A + 1.0Adenosine triphosphate → 1.0D-Carnitinyl-CoA + 1.0Adenosine monophosphate + 1.0Pyrophosphate
ReactionCard

EcoCyc Reactions:

1.0

→

1.0

1.0Coenzyme A + 1.0Carnitine + 1.0Adenosine triphosphate → 1.0L-Carnitinyl-CoA + 1.0Adenosine monophosphate + 1.0Pyrophosphate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Carnitine → 1.0ADP + 1.0L-Carnitinyl-CoA + 1.0Phosphate
ReactionCard

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Carnitine → 1.0ADP + 1.0D-Carnitinyl-CoA + 1.0Phosphate
ReactionCard

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Crotonobetaine → 1.0ADP + 1.0Crotonobetainyl-CoA + 1.0Phosphate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00045	Adenosine monophosphate	MetaboCard
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB01341	ADP	MetaboCard
ECMDB00062	Carnitine	MetaboCard
ECMDB01423	Coenzyme A	MetaboCard
ECMDB21321	Crotonobetaine	MetaboCard
ECMDB20539	Crotonobetainyl-CoA	MetaboCard
ECMDB20541	D-Carnitinyl-CoA	MetaboCard
ECMDB23900	L-Carnitine	MetaboCard
ECMDB20578	L-Carnitinyl-CoA	MetaboCard
ECMDB01429	Phosphate	MetaboCard
ECMDB04142	Pyrophosphate	MetaboCard

GO Classification:

Function
catalytic activity
Process
metabolic process

Gene Properties

Blattner:

b0037

Gene Orientation

Counterclockwise

Centisome Percentage:

0.78

Left Sequence End

36271

Right Sequence End

37824

Gene Sequence:

>1569 bp
ATGGATAGAGGTGCAATGGATATCATTGGCGGACAACATCTACGTCAAATGTGGGACGAT
CTTGCGGACGTTTACGGTCATAAAACGGCGCTGATTTGTGAATCCAGCGGCGGAGTCGTT
AACCGGTATAGTTATCTTGAGTTAAATCAGGAGATTAACCGCACGGCAAACCTGTTTTAT
ACGCTGGGGATTCGCAAAGGCGACAAGGTTGCACTACATCTCGACAACTGCCCGGAATTT
ATCTTTTGCTGGTTCGGGCTGGCAAAAATTGGCGCGATTATGGTGCCGATTAACGCCCGC
CTGTTGTGCGAGGAAAGCGCGTGGATCCTGCAAAATAGCCAGGCGTGCCTGCTGGTGACC
AGTGCGCAATTCTATCCTATGTATCAACAGATTCAGCAGGAAGATGCCACTCAATTGCGG
CACATTTGCCTGACAGATGTGGCACTTCCCGCTGATGATGGCGTGAGTTCGTTTACTCAA
CTGAAAAATCAACAACCTGCCACCTTGTGCTATGCACCGCCGCTATCGACTGACGATACG
GCGGAAATTCTCTTCACCTCCGGCACCACCTCCCGACCGAAAGGTGTGGTGATTACCCAT
TACAACCTGCGCTTCGCTGGATATTACTCCGCCTGGCAGTGTGCACTGCGTGACGATGAC
GTCTACCTGACGGTAATGCCTGCGTTTCATATCGATTGCCAGTGTACTGCGGCGATGGCG
GCGTTTTCTGCCGGGGCCACCTTTGTGCTGGTCGAGAAATACAGCGCCCGCGCCTTCTGG
GGACAGGTACAGAAGTACCGCGCCACCGTTACCGAATGTATTCCGATGATGATCCGTACG
TTGATGGTACAGCCGCCTTCAGCGAACGATCAGCAACACCGCCTGCGGGAAGTGATGTTT
TATCTCAACTTGTCGGAGCAGGAAAAAGATGCGTTTTGTGAACGCTTCGGCGTTCGCTTG
CTGACGTCTTATGGGATGACGGAAACCATTGTGGGCATTATCGGCGATCGTCCTGGCGAT
AAACGACGCTGGCCGTCGATTGGTCGGGTGGGGTTTTGCTACGAAGCGGAGATCCGCGAC
GATCACAATCGCCCGCTCCCGGCTGGTGAGATCGGTGAAATCTGCATTAAAGGCATACCT
GGGAAAACCATCTTCAAAGAGTACTTTCTCAACCCACAAGCCACTGCGAAAGTGCTGGAA
GCCGATGGCTGGCTGCATACCGGCGATACCGGATACCGCGACGAAGAGGACTTTTTTTAT
TTCGTCGATCGCCGCTGCAATATGATTAAACGTGGCGGCGAGAATGTCTCCTGCGTGGAG
CTGGAAAATATTATCGCCGCGCACCCGAAAATTCAGGACATCGTGGTTGTGGGTATTAAA
GATTCGATTCGCGATGAAGCCATCAAAGCATTTGTGGTGCTGAATGAAGGTGAAACATTG
AGCGAAGAGGAATTTTTCCGCTTCTGCGAACAAAATATGGCGAAATTTAAAGTGCCCTCT
TATCTGGAGATCAGAAAAGATCTGCCACGTAATTGCTCGGGGAAAATAATTAGAAAGAAT
CTGAAATAA

Protein Properties

Pfam Domain Function:

AMP-binding (PF00501 )

Protein Residues:

517

Protein Molecular Weight:

58559

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Probable crotonobetaine/carnitine-CoA ligase
MDIIGGQHLRQMWDDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIR
KGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLCEESAWILQNSQACLLVTSAQFY
PMYQQIQQEDATQLRHICLTDVALPADDGVSSFTQLKNQQPATLCYAPPLSTDDTAEILF
TSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG
ATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDQQHRLREVMFYLNLS
EQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRVGFCYEAEIRDDHNRP
LPAGEIGEICIKGIPGKTIFKEYFLNPQATAKVLEADGWLHTGDTGYRDEEDFFYFVDRR
CNMIKRGGENVSCVELENIIAAHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEF
FRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK

References

External Links:

Resource	Link
Uniprot ID:	P31552
Uniprot Name:	CAIC_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	21321919
Ecogene ID:	EG11558
Ecocyc:	EG11558
ColiBase:	b0037
Kegg Gene:	b0037
EchoBASE ID:	EB1519
CCDB:	CAIC_ECOLI
BacMap:	221800780

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
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
Heider, J. (2001). "A new family of CoA-transferases." FEBS Lett 509:345-349. Pubmed: 11749953
Lenski, R. E., Winkworth, C. L., Riley, M. A. (2003). "Rates of DNA sequence evolution in experimental populations of Escherichia coli during 20,000 generations." J Mol Evol 56:498-508. Pubmed: 12664169
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