|Gene:||hisB||Accession Numbers: EG10445 (EcoCyc), b2022, ECK2017|
Subunit composition of imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase = [HisB]2
The bifunctional imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (HisB) carries out the sixth and eighth step of histidine biosynthesis. HisB catalyzes two key reactions in histidine biosynthesis. The first is dehydration of D-erythro-imidazole-glycerol-phosphate to yield imidazole acetol-phosphate [Parker95]. The second is a phosphatase reaction that converts L-histidinol-phosphate into histidinol [Grisolia82].
Much initial work was done on the gene and enzyme from Salmonella typhimurium. The two enzymatic activities were found to reside in distinct domains of the enzyme. The amino-terminal end was shown to have histidinol phosphate phosphatase activity, while the carboxy-terminal domain catalyzed the dehydration of imidazole glycerol-3-phosphate [Loper61, Brady73, Houston74, Chumley81]. A model for the evolution of the bifunctional hisB gene has been proposed [Brilli04].
The amino-terminal domain of HisB (HisB-N) belongs to the superfamily of haloacid dehalogenase (HAD)-like hydrolases. Using a variety of possible substrates (not including histidinol phosphate), no phosphatase activity was detected; thus, the enzyme may be highly substrate-specific. [Kuznetsova06]
Crystal structures of HisB-N isolated from E. coli O157:H7 have been solved and the functional significance of its metal ion requirements elucidated. A catalytic mechanism differing from that of other HAD-like hydrolases has been proposed [Rangarajan06].
A high-throughput study of protein complexes in E. coli has identified HisB as a homomultimeric protein [Lasserre06]. The E. coli O157:H7 HisB-N is a dimer both in solution and the crystal structure. The full-length HisB protein associates into large oligomers; the authors suggest that the basic unit of HisB is a hexamer [Rangarajan06].
|Map Position: [2,091,492 -> 2,092,559] (45.08 centisomes, 162°)||Length: 1068 bp / 355 aa|
Molecular Weight of Polypeptide: 40.278 kD (from nucleotide sequence), 40.5 kD (experimental) [Carlomagno88 ]
Unification Links: ASAP:ABE-0006720 , CGSC:635 , DIP:DIP-9901N , EchoBASE:EB0440 , EcoGene:EG10445 , EcoliWiki:b2022 , ModBase:P06987 , OU-Microarray:b2022 , PortEco:hisB , PR:PRO_000022892 , Pride:P06987 , Protein Model Portal:P06987 , RefSeq:NP_416526 , RegulonDB:EG10445 , SMR:P06987 , String:511145.b2022 , UniProt:P06987
Relationship Links: InterPro:IN-FAMILY:IPR000807 , InterPro:IN-FAMILY:IPR005954 , InterPro:IN-FAMILY:IPR006543 , InterPro:IN-FAMILY:IPR006549 , InterPro:IN-FAMILY:IPR013954 , InterPro:IN-FAMILY:IPR020565 , InterPro:IN-FAMILY:IPR020566 , InterPro:IN-FAMILY:IPR020568 , InterPro:IN-FAMILY:IPR023214 , Panther:IN-FAMILY:PTHR23133:SF2 , PDB:IN-FAMILY:2FPR , PDB:IN-FAMILY:2FPS , PDB:IN-FAMILY:2FPU , PDB:IN-FAMILY:2FPW , PDB:IN-FAMILY:2FPX , Pfam:IN-FAMILY:PF00475 , Pfam:IN-FAMILY:PF08645 , Prosite:IN-FAMILY:PS00954 , Prosite:IN-FAMILY:PS00955
In Paralogous Gene Group: 64 (3 members)
|Biological Process:||GO:0000105 - histidine biosynthetic process
[UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, Parker95]
GO:0016311 - dephosphorylation [GOA06, GOA01, GOA01a, Grisolia82]
GO:0008152 - metabolic process [UniProtGOA11a]
GO:0008652 - cellular amino acid biosynthetic process [UniProtGOA11a]
|Molecular Function:||GO:0004401 - histidinol-phosphatase activity
[GOA06, GOA01, GOA01a, Grisolia82]
GO:0004424 - imidazoleglycerol-phosphate dehydratase activity [GOA06, GOA01, GOA01a, Parker95]
GO:0005515 - protein binding [Rajagopala14]
GO:0042802 - identical protein binding [Rajagopala14]
GO:0003824 - catalytic activity [UniProtGOA11a]
GO:0016787 - hydrolase activity [UniProtGOA11a]
GO:0016791 - phosphatase activity [GOA01a]
GO:0016829 - lyase activity [UniProtGOA11a]
|Cellular Component:||GO:0005737 - cytoplasm
[UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]
GO:0005829 - cytosol [DiazMejia09]
|MultiFun Terms:||metabolism → biosynthesis of building blocks → amino acids → histidine|
|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]
Enzymatic reaction of: imidazoleglycerol-phosphate dehydratase
Synonyms: D-erythro imidazoleglycerol-phosphate dehydratase-histidinol phosphate phosphatase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is irreversible in the direction shown.
The abbreviation IGP is used commonly for imidazoleglycerol-phosphate. This is not to be confused with the IGP of the tryptophan pathway in which IGP signifies indole glycerol-phosphate.
Cofactors or Prosthetic Groups: Mg2+
Alternative Cofactors for Mg2+: Mn2+
Enzymatic reaction of: histidinol-phosphatase
Synonyms: histidinolphosphate phosphatase, L-Histidinol-phosphate phosphohydrolase, HPase, HAD21
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is irreversible in the direction shown.
Cofactors or Prosthetic Groups: Mg2+
|Protein-Segment||1 -> 166|
|Protein-Segment||167 -> 355|
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 b2022 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10445; confirmed by SwissProt match.
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
Brady73: Brady DR, Houston LL (1973). "Some properties of the catalytic sites of imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase, a bifunctional enzyme from Salmonella typhimurium." J Biol Chem 1973;248(7);2588-92. PMID: 4349042
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
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
Kuznetsova06: Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF (2006). "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family." J Biol Chem 281(47):36149-61. PMID: 16990279
Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726
Parker95: Parker, A.R., Moore, J.A., Schwab, J.M., Davisson, V.J. (1995). "Escherichia coli Imidazoleglycerol Phosphate Dehydratase: Spectroscopic Characterization of the Enzymic Product and the Steric Course of the Reaction." Journal of the American Chemical Society.
Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554
Rangarajan06: Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M (2006). "Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway." J Biol Chem 281(49):37930-41. PMID: 16966333
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
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
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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