Escherichia coli K-12 substr. MG1655 Enzyme: histidinol-phosphate aminotransferase

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

Regulation Summary Diagram: ?

Regulation summary diagram for hisC

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].

Gene Citations: [Alifano92]

Locations: cytosol

Map Position: [2,090,422 -> 2,091,492] (45.06 centisomes, 162°)
Length: 1071 bp / 356 aa

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

In Paralogous Gene Group: 163 (5 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for hisC

GO Terms:

Biological Process: GO:0000105 - histidine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, Grisolia85]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004400 - histidinol-phosphate transaminase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Grisolia85]
GO:0042802 - identical protein binding Inferred from experiment [Grisolia85]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0008483 - transaminase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030170 - pyridoxal phosphate binding Inferred by computational analysis [GOA01a]
GO:0080130 - L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids histidine

Essentiality data for hisC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 3]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
No [Feist07, Comment 4]

Curated 13-Mar-2006 by Shearer A , SRI International
Last-Curated ? 03-Oct-2013 by Kubo A , SRI International

Enzymatic reaction of: histidinol-phosphate aminotransferase

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

EC Number:

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

Sequence Features

Protein sequence of HisC with features indicated

Feature Class Location Citations Comment
Sequence-Conflict 130
[Grisolia85, Carlomagno88, UniProt10a]
UniProt: (in Ref. 1 and 2);
Sequence-Conflict 149
[Grisolia85, Carlomagno88, UniProt10a]
UniProt: (in Ref. 1 and 2);
N6-pyridoxal-phosphate-Lys-Modification 214
UniProt: N6-(pyridoxal phosphate)lysine.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b2021 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10446; confirmed by SwissProt match.


Alifano92: Alifano P, Carlomagno MS, Bruni CB (1992). "Location of the hisGDCBHAFI operon on the physical map of Escherichia coli." J Bacteriol 1992;174(11);3830-1. PMID: 1592835

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

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

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

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."

Goldschmidt70: Goldschmidt EP, Cater MS, Matney TS, Butler MA, Greene A (1970). "Genetic analysis of the histidine operon in Escherichia coli K12." Genetics 66(2);219-29. PMID: 4934197

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

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

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

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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."

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

Other References Related to Gene Regulation

Di78: Di Nocera PP, Blasi F, Di Lauro R, Frunzio R, Bruni CB (1978). "Nucleotide sequence of the attenuator region of the histidine operon of Escherichia coli K-12." Proc Natl Acad Sci U S A 75(9);4276-80. PMID: 360215

Frunzio81: Frunzio R, Bruni CB, Blasi F (1981). "In vivo and in vitro detection of the leader RNA of the histidine operon of Escherichia coli K-12." Proc Natl Acad Sci U S A 78(5);2767-71. PMID: 6166940

Lee12: Lee JH, Lennon CW, Ross W, Gourse RL (2012). "Role of the coiled-coil tip of Escherichia coli DksA in promoter control." J Mol Biol 416(4);503-17. PMID: 22200485

Verde81: Verde P, Frunzio R, di Nocera PP, Blasi F, Bruni CB (1981). "Identification, nucleotide sequence and expression of the regulatory region of the histidine operon of Escherichia coli K-12." Nucleic Acids Res 9(9);2075-86. PMID: 6170941

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Oct 13, 2015, biocyc13.