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MetaCyc Enzyme: N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase

Gene: hisA Accession Numbers: EG10444 (MetaCyc), b2024, ECK2019

Species: Escherichia coli K-12 substr. MG1655

Summary:
N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase (HisA) carries out the fourth step in histidine biosynthesis.

HisA catalyzes an internal redox reaction known as an Amadori rearrangement [HennSax02].

Spontaneous hisA mutants were investigated [Jankovic90].

Locations: cytosol

Map Position: [2,093,149 -> 2,093,886]

Molecular Weight of Polypeptide: 26.033 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006725 , CGSC:636 , EchoBASE:EB0439 , EcoGene:EG10444 , EcoliWiki:b2024 , ModBase:P10371 , OU-Microarray:b2024 , PortEco:hisA , PR:PRO_000022891 , Pride:P10371 , Protein Model Portal:P10371 , RefSeq:NP_416528 , RegulonDB:EG10444 , SMR:P10371 , String:511145.b2024 , UniProt:P10371

Relationship Links: InterPro:IN-FAMILY:IPR006062 , InterPro:IN-FAMILY:IPR006063 , InterPro:IN-FAMILY:IPR011060 , InterPro:IN-FAMILY:IPR013785 , InterPro:IN-FAMILY:IPR023016 , Pfam:IN-FAMILY:PF00977

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0000105 - histidine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, HennSax02]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003949 - 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, HennSax02]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids histidine

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


Enzymatic reaction of: N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase

Synonyms: N-(5'-phospho-D-ribosylformimino-5-amino-1-(5'-phosphoribosyl)-4-imidazole carboxamide isomerase, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, phosphoribosylformiminophoshoribosylaminoimidazolecarboamide ketolisomerase, phosphoribosylformimino-5-amino-1-phosphoribosyl-4-imidazole carboxamide isomerase, phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase

EC Number: 5.3.1.16

1-(5-phospho-β-D-ribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide <=> phosphoribulosylformimino-AICAR-P

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of histidine, purine, and pyrimidine biosynthesis , histidine biosynthesis

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


Sequence Features

Feature Class Location Citations Comment
Active-Site 7
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 84
[Carlomagno88, UniProt10]
Alternate sequence: T; UniProt: (in Ref. 1; CAA31816);
Sequence-Conflict 126
[Carlomagno88, UniProt10]
Alternate sequence: V; UniProt: (in Ref. 1; CAA31816);
Active-Site 129
[UniProt10a]
UniProt: Proton donor; Non-Experimental Qualifier: by similarity;

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
10/20/97 Gene b2024 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10444; confirmed by SwissProt match.


References

Carlomagno88: Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB (1988). "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." J Mol Biol 1988;203(3);585-606. PMID: 3062174

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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

HennSax02: Henn-Sax M, Thoma R, Schmidt S, Hennig M, Kirschner K, Sterner R (2002). "Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates." Biochemistry 41(40);12032-42. PMID: 12356303

Jankovic90: Jankovic M, Kostic T, Savic DJ (1990). "DNA sequence analysis of spontaneous histidine mutations in a polA1 strain of Escherichia coli K12 suggests a specific role of the GTGG sequence." Mol Gen Genet 223(3);481-6. PMID: 2270088

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Matney64: Matney TS, Goldschmidt EP, Erwin NS, Scroggs RA (1964). "A preliminary map of genomic sites for F-attachment in Escherichia coli K12." Biochem Biophys Res Commun 17(3);278-81. PMID: 5324449

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." 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."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."


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 22, 2014, BIOCYC14B.