|Gene:||hisC||Accession Numbers: EG10446 (MetaCyc), b2021, ECK2016|
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of histidinol-phosphate aminotransferase = [HisC]2
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].
|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
|Biological Process:||GO:0000105 - histidine biosynthetic process
[UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, Grisolia85]
GO:0008152 - metabolic process [GOA01a]
GO:0008652 - cellular amino acid biosynthetic process [UniProtGOA11a]
GO:0009058 - biosynthetic process [GOA01a]
|Molecular Function:||GO:0004400 - histidinol-phosphate transaminase activity
[GOA06, GOA01, GOA01a, Grisolia85]
GO:0042802 - identical protein binding [Grisolia85]
GO:0003824 - catalytic activity [GOA01a]
GO:0008483 - transaminase activity [UniProtGOA11a]
GO:0016740 - transferase activity [UniProtGOA11a, GOA01a]
GO:0030170 - pyridoxal phosphate binding [GOA01a]
GO:0080130 - L-phenylalanine:2-oxoglutarate aminotransferase activity [GOA01]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09, Ishihama08]|
|MultiFun Terms:||metabolism → biosynthesis of building blocks → amino acids → histidine|
Enzymatic reaction of: histidinol-phosphate aminotransferase
Synonyms: imidazolylacetolphosphate aminotransferase, histidinol-phosphate transaminase, imidazolylacetolphosphate:L-glutamate aminotransferase
EC Number: 220.127.116.11
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.
10/20/97 Gene b2021 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10446; confirmed by SwissProt match.
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
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
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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493