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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: apo-citrate lyase phosphoribosyl-dephospho-CoA transferase

Gene: citX Accession Numbers: G6340 (MetaCyc), b0614, ECK0607

Synonyms: ybdU

Species: Escherichia coli K-12 substr. MG1655

Summary:
CitX catalyzes the transfer of the citrate lyase prosthetic group 2'-(5''-phosphoribosyl)-3'-dephospho-CoA to the apo-ACP protein of citrate lyase, CitD, converting it to the active holo-ACP form [Schneider00, Schneider00a]. In vitro, the enzyme also functions as a nucleotidyltransferase [Schneider00].

Citations: [Hoenke00]

Locations: cytosol

Map Position: [646,707 <- 647,258]

Molecular Weight of Polypeptide: 20.27 kD (from nucleotide sequence), 20.0 kD (experimental) [Schneider00 ]

Unification Links: ASAP:ABE-0002116 , EchoBASE:EB3310 , EcoGene:EG13540 , EcoliWiki:b0614 , OU-Microarray:b0614 , PortEco:citX , PR:PRO_000022293 , Pride:P0A6G5 , Protein Model Portal:P0A6G5 , RefSeq:NP_415147 , RegulonDB:G6340 , String:511145.b0614 , UniProt:P0A6G5

Relationship Links: InterPro:IN-FAMILY:IPR005551 , Pfam:IN-FAMILY:PF03802

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0018247 - protein-phosphoribosyl dephospho-coenzyme A linkage Inferred from experiment [Schneider00]
GO:0051191 - prosthetic group biosynthetic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0050519 - holo-citrate lyase synthase activity Inferred from experiment Inferred by computational analysis [GOA01, Schneider00, Schneider00a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer protein related posttranslational modification

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: apo-citrate lyase phosphoribosyl-dephospho-CoA transferase

Synonyms: 2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase, holo-citrate lyase synthase

EC Number: 2.7.7.61

2'-(5''-triphospho-α-D-ribosyl)-3'-dephospho-CoA + [an apo citrate-lyase acyl-carrier protein] <=> [a holo citrate lyase acyl-carrier protein] + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for 2'-(5''-triphospho-α-D-ribosyl)-3'-dephospho-CoA: ATP [Schneider00 ]

In Pathways: citrate lyase activation

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hoenke00: Hoenke S, Schmid M, Dimroth P (2000). "Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases." Biochemistry 39(43);13233-40. PMID: 11052676

Schneider00: Schneider K, Dimroth P, Bott M (2000). "Biosynthesis of the prosthetic group of citrate lyase." Biochemistry 2000;39(31);9438-50. PMID: 10924139

Schneider00a: Schneider K, Dimroth P, Bott M (2000). "Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group." FEBS Lett 2000;483(2-3);165-8. PMID: 11042274

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 29, 2014, biocyc13.