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MetaCyc Enzyme: histidinol-phosphate aminotransferase

Gene: hisC Accession Numbers: EG10446 (MetaCyc), b2021, ECK2016

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of histidinol-phosphate aminotransferase = [HisC]2

Summary:
Histidinol-phosphate aminotransferase (HisC) catalyzes the seventh step in the biosynthesis of histidine. HisC catalyzes the conversion of imidazole acetol-phosphate to histidinol-phosphate [Grisolia85].

A number of crystal structures have been determined for the functional HisC dimer. HisC has been crystallized on its own to 2 Å, with histidinol-phosphate to 2.2 Å and with N-(5'-phosphopyridoxyl)-L-glutamate to 2.3 Å [Haruyama01]. It has also been crystallized with pyridoxamine-5'-phosphate to 1.5 Å, as an internal aldimine with pyridoxal-5'-phosphate to 2.2 Å and in a covalent complex with pyridoxal-5'-phosphate and L-histidinol to 2.2 Å [Sivaraman01].

Spectroscopic and pK(a) analyses of HisC have also been carried out [Mizuguchi03].

HisC expression levels were elevated when grown anaerobically at high pH [Yohannes04].

Locations: cytosol

Map Position: [2,090,422 -> 2,091,492]

Molecular Weight of Polypeptide: 39.36 kD (from nucleotide sequence), 38.5 kD (experimental) [Grisolia85 ]

Molecular Weight of Multimer: 80.0 kD (experimental) [Sivaraman01]

Unification Links: ASAP:ABE-0006717 , CGSC:634 , DIP:DIP-9902N , EchoBASE:EB0441 , EcoGene:EG10446 , EcoliWiki:b2021 , Mint:MINT-1322565 , ModBase:P06986 , OU-Microarray:b2021 , PortEco:hisC , PR:PRO_000022893 , Protein Model Portal:P06986 , RefSeq:NP_416525 , RegulonDB:EG10446 , SMR:P06986 , String:511145.b2021 , UniProt:P06986

Relationship Links: InterPro:IN-FAMILY:IPR001917 , InterPro:IN-FAMILY:IPR004839 , InterPro:IN-FAMILY:IPR005861 , InterPro:IN-FAMILY:IPR015421 , InterPro:IN-FAMILY:IPR015422 , InterPro:IN-FAMILY:IPR015424 , PDB:Structure:1FG3 , PDB:Structure:1FG7 , PDB:Structure:1GEW , PDB:Structure:1GEX , PDB:Structure:1GEY , PDB:Structure:1IJI , Pfam:IN-FAMILY:PF00155 , Prosite:IN-FAMILY:PS00599

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0000105 - histidine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA06, GOA01, Grisolia85]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0004400 - histidinol-phosphate transaminase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Grisolia85]
GO:0042802 - identical protein binding Inferred from experiment [Grisolia85]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0008483 - transaminase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0030170 - pyridoxal phosphate binding Inferred by computational analysis [GOA01]
GO:0080130 - L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids histidine

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Enzymatic reaction of: histidinol-phosphate aminotransferase

Synonyms: imidazolylacetolphosphate aminotransferase, histidinol-phosphate transaminase, imidazolylacetolphosphate:L-glutamate aminotransferase

EC Number: 2.6.1.9

imidazole acetol-phosphate + L-glutamate <=> L-histidinol-phosphate + 2-oxoglutarate

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 , L-histidine biosynthesis

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 130
[Grisolia85, Carlomagno88, UniProt10]
UniProt: (in Ref. 1 and 2);
Sequence-Conflict 149
[Grisolia85, Carlomagno88, UniProt10]
UniProt: (in Ref. 1 and 2);
N6-pyridoxal-phosphate-Lys-Modification 214
[UniProt11]
UniProt: N6-(pyridoxal phosphate)lysine.

History:
10/20/97 Gene b2021 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10446; 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, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Grisolia85: Grisolia V, Carlomagno MS, Nappo AG, Bruni CB (1985). "Cloning, structure, and expression of the Escherichia coli K-12 hisC gene." J Bacteriol 1985;164(3);1317-23. PMID: 2999081

Haruyama01: Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H (2001). "Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme." Biochemistry 40(15);4633-44. PMID: 11294630

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Mizuguchi03: Mizuguchi H, Hayashi H, Miyahara I, Hirotsu K, Kagamiyama H (2003). "Characterization of histidinol phosphate aminotransferase from Escherichia coli." Biochim Biophys Acta 1647(1-2);321-4. PMID: 12686152

Sivaraman01: Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A (2001). "Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate." J Mol Biol 311(4);761-76. PMID: 11518529

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

UniProt11: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11: 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."

Yohannes04: Yohannes E, Barnhart DM, Slonczewski JL (2004). "pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12." J Bacteriol 186(1);192-9. PMID: 14679238


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 19.0 on Fri May 22, 2015, BIOCYC14B.