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MetaCyc Protein: citrate lyase, citryl-ACP lyase component

Gene: citE Accession Numbers: G6342 (MetaCyc), b0616, ECK0609

Synonyms: ybdW

Species: Escherichia coli K-12 substr. MG1655

Component of: citrate lyase, inactive

Subunit composition of citrate lyase, citryl-ACP lyase component = [CitE]6
         citrate lyase, citryl-ACP lyase β subunit = CitE

Alternative forms of citrate lyase, inactive: citrate lyase (extended summary available)

Locations: cytosol

Map Position: [648,805 <- 649,713]

Molecular Weight of Polypeptide: 33.11 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0002122, DIP:DIP-9285N, EchoBASE:EB3312, EcoGene:EG13542, EcoliWiki:b0616, Mint:MINT-1283346, ModBase:P0A9I1, OU-Microarray:b0616, PortEco:citE, PR:PRO_000022290, Pride:P0A9I1, Protein Model Portal:P0A9I1, RefSeq:NP_415149, RegulonDB:G6342, SMR:P0A9I1, String:511145.b0616, UniProt:P0A9I1

Relationship Links: InterPro:IN-FAMILY:IPR005000, InterPro:IN-FAMILY:IPR006475, InterPro:IN-FAMILY:IPR011206, InterPro:IN-FAMILY:IPR015813, Pfam:IN-FAMILY:PF03328

Gene-Reaction Schematic

Gene-Reaction Schematic


GO Terms:
Biological Process:
Inferred by computational analysisGO:0006084 - acetyl-CoA metabolic process [GOA01a]
Molecular Function:
Inferred by computational analysisGO:0003824 - catalytic activity [GOA01a]
Inferred by computational analysisGO:0008815 - citrate (pro-3S)-lyase activity [GOA01]
Inferred by computational analysisGO:0008816 - citryl-CoA lyase activity [GOA01, GOA01a]
Inferred by computational analysisGO:0016829 - lyase activity [UniProtGOA11a]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11a]
Cellular Component:
Inferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a]
Inferred by computational analysisGO:0005829 - cytosol [DiazMejia09]
Inferred by computational analysisGO:0009346 - citrate lyase complex [GOA01a]

MultiFun Terms: metabolismcentral intermediary metabolismunassigned reversible reactions

Credits:
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International


Subunit of: citrate lyase, inactive

Synonyms: (HS)-citrate lyase, citrate lyase, thiol form, deacetyl-citrate lyase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of citrate lyase, inactive = [(CitD)6][(CitF)6][(CitE)6]
         citrate lyase [acyl carrier protein] component = (CitD)6 (summary available)
                 citrate lyase, acyl carrier γ subunit = CitD
         citrate lyase, citrate-ACP transferase component = (CitF)6
                 citrate lyase, citrate-ACP transferase α subunit = CitF
         citrate lyase, citryl-ACP lyase component = (CitE)6
                 citrate lyase, citryl-ACP lyase β subunit = CitE

Reactions known to consume the compound:

citrate lyase activation :
[a holo citrate lyase acyl-carrier protein] + acetate + ATP → an acetyl-[holo citrate lyase acyl-carrier protein] + AMP + diphosphate
[a holo citrate lyase acyl-carrier protein] + S-acetyl phosphopantetheine → an acetyl-[holo citrate lyase acyl-carrier protein] + 4'-phosphopantetheine

Reactions known to produce the compound:

citrate lyase activation :
an acetyl-[holo citrate lyase acyl-carrier protein] + H2O → [a holo citrate lyase acyl-carrier protein] + acetate + H+
2'-(5''-triphospho-α-D-ribosyl)-3'-dephospho-CoA + [a citrate-lyase acyl-carrier protein] → [a holo citrate lyase acyl-carrier protein] + diphosphate + H+

Credits:
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 76
Inferred by computational analysis[UniProt15]
UniProt: Substrate.
Metal-Binding-Site 139
Inferred by computational analysis[UniProt15]
UniProt: Magnesium.
Sequence-Conflict 150 -> 156
Inferred by curator[UniProt15]
UniProt: (in Ref. 5; AAC28948).
Metal-Binding-Site 166
Inferred by computational analysis[UniProt15]
UniProt: Magnesium.

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06].
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."

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

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 Pathway Tools version 19.5 (software by SRI International) on Fri Apr 29, 2016, biocyc13.