Identification |
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Name: | Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase |
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Synonyms: | - Apo-ACP nucleodityltransferase
- Holo-ACP synthase
- Holo-citrate lyase synthase
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Gene Name: | citX |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in prosthetic group biosynthetic process |
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Specific Function: | Transfers 2-(5''-triphosphoribosyl)-3'- dephosphocoenzyme-A on a serine residue to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield holo-acyl carrier protein |
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Cellular Location: | Not Available |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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KEGG Reactions: | | | |
1.0 | ↔ | 1.0 |
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SMPDB Reactions: | |
1.0 | + | 1.0 [an apo citrate-lyase acyl-carrier protein] | → | 1.0Pyrophosphate | + | 1.0 | + | 1.0[a holo citrate lyase acyl-carrier protein] |
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EcoCyc Reactions: | |
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Complex Reactions: | |
1.0 | + | 1.0citrate lyase apo-[acyl-carrier-protein] | → | 1.0citrate lyase holo-[acyl-carrier-protein] | + | 1.0 |
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Metabolites: | |
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GO Classification: | Process |
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biosynthetic process | cellular biosynthetic process | cofactor biosynthetic process | metabolic process | prosthetic group biosynthetic process |
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Gene Properties |
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Blattner: | b0614 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 13.94 |
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Left Sequence End | 646707 |
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Right Sequence End | 647258 |
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Gene Sequence: | >552 bp
ATGTTGTTAGAACAGGGGTGGCTGGTTGGCGCGCGCCGCGTTCCCTCACCACATTACGAT
TGCCGCCCGGATGACGAAACACCCACCCTGCTGGTGGTGCACAATATTAGCCTGCCGCCA
GGCGAGTTTGGCGGTCCGTGGATCGACGCATTATTCACTGGAACTATTGATCCGCAGGCA
CATCCTTTCTTTGCTGAGATCGCCCATTTGCGCGTCTCCGCTCACTGTTTGATTCGCCGT
GATGGTGAAATAGTCCAGTATGTTCCTTTCGATAAACGTGCATGGCATGCGGGAGTCTCT
CAGTATCAGGGGCGCGAACGCTGCAATGATTTTTCTATTGGGATTGAGCTTGAAGGCACC
GATACGCTGGCGTATACCGATGCGCAGTATCAACAGCTTGCGGCGGTTACGCGGGCACTG
ATTGATTGCTATCCGGATATCGCTAAAAACATGACGGGCCATTGTGATATTGCGCCGGAT
CGGAAAACCGATCCCGGTCCTGCATTTGATTGGGCACGGTTTCGTGTGCTGGTCAGCAAG
GAGACAACATGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 183 |
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Protein Molecular Weight: | 20270 |
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Protein Theoretical pI: | 7 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase
MHLLPELASHHAVSIPELLVSRDERQARQHVWLKRHPVPLVSFTVVAPGPIKDSEVTRRI
FNHGVTALRALAAKQGWQIQEQAALVSASGPEGMLSIAAPARDLKLATIELEHSHPLGRL
WDIDVLTPEGEILSRRDYSLPPRRCLLCEQSAAVCARGKTHQLTDLLNRMEALLNDVDAC
NVN |
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References |
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External Links: | |
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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
- 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
- Pos, K. M., Dimroth, P., Bott, M. (1998). "The Escherichia coli citrate carrier CitT: a member of a novel eubacterial transporter family related to the 2-oxoglutarate/malate translocator from spinach chloroplasts." J Bacteriol 180:4160-4165. Pubmed: 9696764
- Schneider, K., Dimroth, P., Bott, M. (2000). "Biosynthesis of the prosthetic group of citrate lyase." Biochemistry 39:9438-9450. Pubmed: 10924139
- Schneider, K., Dimroth, P., Bott, M. (2000). "Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group." FEBS Lett 483:165-168. Pubmed: 11042274
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