EzCatDB: T00232

DB codeT00232
CATH domainDomain 13.40.50.10490Catalytic domain
Domain 23.40.50.10490Catalytic domain
Domain 31.10.1390.10Catalytic domain
E.C.5.3.1.9
CSA1dqr

CATH domainRelated DB codes (homologues)
3.40.50.10490T00201

Enzyme Name
Swiss-protKEGG

P13376Q9N1E2P08059P06744
Protein nameGlucose-6-phosphate isomerase BGlucose-6-phosphate isomeraseGlucose-6-phosphate isomeraseGlucose-6-phosphate isomeraseglucose-6-phosphate isomerase
phosphohexose isomerase
phosphohexomutase
oxoisomerase
hexosephosphate isomerase
phosphosaccharomutase
phosphoglucoisomerase
phosphohexoisomerase
phosphoglucose isomerase
glucose phosphate isomerase
hexose phosphate isomerase
D-glucose-6-phosphate ketol-isomerase
SynonymsGPI B
EC 5.3.1.9
Phosphoglucose isomerase B
PGI-B
Phosphohexose isomerase B
PHI-B
GPI
EC 5.3.1.9
Phosphoglucose isomerase
PGI
Phosphohexose isomerase
PHI
GPI
EC 5.3.1.9
Phosphoglucose isomerase
PGI
Phosphohexose isomerase
PHI
GPI
EC 5.3.1.9
Phosphoglucose isomerase
PGI
Phosphohexose isomerase
PHI
Neuroleukin
NLK
Sperm antigen 36
SA-36

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00030Pentose phosphate pathway
MAP00500Starch and sucrose metabolism

Swiss-prot:Accession NumberP13376Q9N1E2P08059P06744
Entry nameG6PIB_BACSTG6PI_RABITG6PI_PIGG6PI_HUMAN
ActivityD-glucose 6-phosphate = D-fructose 6- phosphate.D-glucose 6-phosphate = D-fructose 6- phosphate.D-glucose 6-phosphate = D-fructose 6- phosphate.D-glucose 6-phosphate = D-fructose 6- phosphate.
SubunitHomodimer.Homodimer.Homodimer.Homodimer.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.Cytoplasm.
Cofactor





SubstratesProductsintermediates
KEGG-idC00092C00085

CompoundD-Glucose 6-phosphateD-Fructose 6-phosphateIntermediate-1Intermediate-2
Typecarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ion

1b0zA01UnboundUnboundUnboundUnbound
1c7qA01UnboundUnboundUnboundUnbound
1c7rA01UnboundUnboundUnboundIntermediate-analogue:PA5
2pgiA01UnboundUnboundUnboundUnbound
1dqrA01UnboundUnboundIntermediate-analogue:6PGUnbound
1dqrB01UnboundUnboundIntermediate-analogue:6PGUnbound
1g98A01UnboundUnboundUnboundIntermediate-analogue:PA5
1g98B01UnboundUnboundUnboundIntermediate-analogue:PA5
1hm5A01UnboundUnboundUnboundUnbound
1hm5B01UnboundUnboundUnboundUnbound
1hoxA01UnboundBound:F6PUnboundUnbound
1hoxB01UnboundBound:F6PUnboundUnbound
1kojA01UnboundUnboundUnboundIntermediate-analogue:PAN
1kojB01UnboundUnboundUnboundIntermediate-analogue:PAN
1n8tA01UnboundUnboundUnboundUnbound
1n8tB01UnboundUnboundUnboundUnbound
1gzdA01UnboundUnboundUnboundUnbound
1gzvA01UnboundUnboundUnboundIntermediate-analogue:PA5
1iatA01UnboundUnboundUnboundUnbound
1iriA01UnboundUnboundUnboundIntermediate-analogue:E4P
1iriB01UnboundUnboundUnboundIntermediate-analogue:E4P
1iriC01UnboundUnboundUnboundIntermediate-analogue:E4P
1iriD01UnboundUnboundUnboundIntermediate-analogue:E4P
1jiqA01UnboundUnboundUnboundUnbound
1jiqB01UnboundUnboundUnboundUnbound
1jiqC01UnboundUnboundUnboundUnbound
1jiqD01UnboundUnboundUnboundUnbound
1jlhA01UnboundUnboundUnboundUnbound
1jlhB01UnboundUnboundUnboundUnbound
1jlhC01UnboundUnboundUnboundUnbound
1jlhD01UnboundUnboundUnboundUnbound
1nuhA01UnboundUnboundUnboundIntermediate-analogue:PA5
1b0zA02UnboundUnboundUnboundUnbound
1c7qA02UnboundUnboundUnboundUnbound
1c7rA02UnboundUnboundUnboundUnbound
2pgiA02UnboundUnboundUnboundUnbound
1dqrA02UnboundUnboundUnboundUnbound
1dqrB02UnboundUnboundUnboundUnbound
1g98A02UnboundUnboundUnboundUnbound
1g98B02UnboundUnboundUnboundUnbound
1hm5A02UnboundUnboundUnboundUnbound
1hm5B02UnboundUnboundUnboundUnbound
1hoxA02UnboundUnboundUnboundUnbound
1hoxB02UnboundUnboundUnboundUnbound
1kojA02UnboundUnboundUnboundUnbound
1kojB02UnboundUnboundUnboundUnbound
1n8tA02UnboundUnboundUnboundUnbound
1n8tB02UnboundUnboundUnboundUnbound
1gzdA02UnboundUnboundUnboundUnbound
1gzvA02UnboundUnboundUnboundUnbound
1iatA02UnboundUnboundUnboundUnbound
1iriA02UnboundUnboundUnboundUnbound
1iriB02UnboundUnboundUnboundUnbound
1iriC02UnboundUnboundUnboundUnbound
1iriD02UnboundUnboundUnboundUnbound
1jiqA02UnboundUnboundUnboundUnbound
1jiqB02UnboundUnboundUnboundUnbound
1jiqC02UnboundUnboundUnboundUnbound
1jiqD02UnboundUnboundUnboundUnbound
1jlhA02UnboundUnboundUnboundUnbound
1jlhB02UnboundUnboundUnboundUnbound
1jlhC02UnboundUnboundUnboundUnbound
1jlhD02UnboundUnboundUnboundUnbound
1nuhA02UnboundUnboundUnboundUnbound
1b0zA03UnboundUnboundUnboundUnbound
1c7qA03UnboundUnboundUnboundUnbound
1c7rA03UnboundUnboundUnboundUnbound
2pgiA03UnboundUnboundUnboundUnbound
1dqrA03UnboundUnboundUnboundUnbound
1dqrB03UnboundUnboundUnboundUnbound
1g98A03UnboundUnboundUnboundUnbound
1g98B03UnboundUnboundUnboundUnbound
1hm5A03UnboundUnboundUnboundUnbound
1hm5B03UnboundUnboundUnboundUnbound
1hoxA03UnboundUnboundUnboundUnbound
1hoxB03UnboundUnboundUnboundUnbound
1kojA03UnboundUnboundUnboundUnbound
1kojB03UnboundUnboundUnboundUnbound
1n8tA03UnboundUnboundUnboundUnbound
1n8tB03UnboundUnboundUnboundUnbound
1gzdA03UnboundUnboundUnboundUnbound
1gzvA03UnboundUnboundUnboundUnbound
1iatA03UnboundUnboundUnboundUnbound
1iriA03UnboundUnboundUnboundUnbound
1iriB03UnboundUnboundUnboundUnbound
1iriC03UnboundUnboundUnboundUnbound
1iriD03UnboundUnboundUnboundUnbound
1jiqA03UnboundUnboundUnboundUnbound
1jiqB03UnboundUnboundUnboundUnbound
1jiqC03UnboundUnboundUnboundUnbound
1jiqD03UnboundUnboundUnboundUnbound
1jlhA03UnboundUnboundUnboundUnbound
1jlhB03UnboundUnboundUnboundUnbound
1jlhC03UnboundUnboundUnboundUnbound
1jlhD03UnboundUnboundUnboundUnbound
1nuhA03UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P13376 & literature [13]
pdbCatalytic residues
1b0zA01GLU 285;HIS 306
1c7qA01GLU 285;HIS 306
1c7rA01GLU 285;HIS 306
2pgiA01GLU 285;HIS 306
1dqrA01GLU 357;HIS 388
1dqrB01GLU 357;HIS 388
1g98A01GLU 357;HIS 388
1g98B01GLU 357;HIS 388
1hm5A01GLU 357;HIS 388
1hm5B01GLU 357;HIS 388
1hoxA01GLU 357;HIS 388
1hoxB01GLU 357;HIS 388
1kojA01GLU 357;HIS 388
1kojB01GLU 357;HIS 388
1n8tA01GLU 357;HIS 388
1n8tB01GLU 357;HIS 388
1gzdA01GLU 357;HIS 388
1gzvA01GLU 357;HIS 388
1iatA01GLU 357;HIS 388
1iriA01GLU 358;HIS 389
1iriB01GLU 358;HIS 389
1iriC01GLU 358;HIS 389
1iriD01GLU 358;HIS 389
1jiqA01GLU 358;HIS 389
1jiqB01GLU 358;HIS 389
1jiqC01GLU 358;HIS 389
1jiqD01GLU 358;HIS 389
1jlhA01GLU 357;HIS 388
1jlhB01GLU 357;HIS 388
1jlhC01GLU 357;HIS 388
1jlhD01GLU 357;HIS 388
1nuhA01GLU 357;HIS 388
1b0zA02GLU 145
1c7qA02GLU 145
1c7rA02GLU 145
2pgiA02GLU 145
1dqrA02GLU 216
1dqrB02GLU 216
1g98A02GLU 216
1g98B02GLU 216
1hm5A02GLU 216
1hm5B02GLU 216
1hoxA02GLU 216
1hoxB02GLU 216
1kojA02GLU 216
1kojB02GLU 216
1n8tA02GLU 216
1n8tB02GLU 216
1gzdA02GLU 216
1gzvA02GLU 216
1iatA02GLU 216
1iriA02GLU 217
1iriB02GLU 217
1iriC02GLU 217
1iriD02GLU 217
1jiqA02GLU 217
1jiqB02GLU 217
1jiqC02GLU 217
1jiqD02GLU 217
1jlhA02GLU 216
1jlhB02GLU 216
1jlhC02GLU 216
1jlhD02GLU 216
1nuhA02GLU 216
1b0zA03LYS 420
1c7qA03LYS 420
1c7rA03LYS 420
2pgiA03LYS 420
1dqrA03LYS 518
1dqrB03LYS 518
1g98A03LYS 518
1g98B03LYS 518
1hm5A03LYS 518
1hm5B03LYS 518
1hoxA03LYS 518
1hoxB03LYS 518
1kojA03LYS 518
1kojB03LYS 518
1n8tA03LYS 518
1n8tB03LYS 518
1gzdA03LYS 518
1gzvA03LYS 518
1iatA03LYS 518
1iriA03LYS 519
1iriB03LYS 519
1iriC03LYS 519
1iriD03LYS 519
1jiqA03LYS 519
1jiqB03LYS 519
1jiqC03LYS 519
1jiqD03LYS 519
1jlhA03LYS 518
1jlhB03LYS 518
1jlhC03LYS 518
1jlhD03LYS 518
1nuhA03LYS 518

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Fig.1a, p.146-2
[8]Scheme I, Scheme II
[11]Fig.1, p.24422
[12]Fig.3, p.958-9614
[13]Fig.6, p.23158-231605
[15]Fig.4, p.1564-15664
[16]Fig.3B, Fig.4, p.7802-78042
[17]Fig.3, p.12-142
[18]Fig.8, p.455-4584
[23]Fig.7, p.462-4634
[25]p.121-122

references
[1]
JournalJ Mol Biol
Year1977
Volume109
Pages475-85
AuthorsShaw PJ, Muirhead H
TitleCrystallographic Structure Analysis of Glucose-6-Phosphate Isomerase at 3.5 A Resolution.
Related PDB1b0z
[2]
PubMed ID7410429
JournalJ Biol Chem
Year1980
Volume255
Pages9369-74
AuthorsGibson DR, Gracy RW, Hartman FC
TitleAffinity labeling and characterization of the active site histidine of glucosephosphate isomerase. Sequence homology with triosephosphate isomerase.
[3]
PubMed ID6798937
JournalArch Biochem Biophys
Year1981
Volume212
Pages347-59
AuthorsLu HS, Gracy RW
TitleSpecific cleavage of glucosephosphate isomerases at cysteinyl residues using 2-nitro-5-thiocyanobenzoic acid: analyses of peptides eluted from polyacrylamide gels and localization of active site histidyl and lysyl residues.
[4]
PubMed ID7225356
JournalBiochemistry
Year1981
Volume20
Pages1756-61
AuthorsSchnackerz KD, Chirgwin JM, Noltmann EA
TitleSynthesis of 1-chloro-2-oxohexanol 6-phosphate, a covalent active-site reagent for phosphoglucose isomerase.
[5]
PubMed ID6115414
JournalPhilos Trans R Soc Lond B Biol Sci
Year1981
Volume293
Pages145-57
AuthorsAchari A, Marshall SE, Muirhead H, Palmieri RH, Noltmann EA
TitleGlucose-6-phosphate isomerase.
[6]
PubMed ID6762366
JournalIsozymes Curr Top Biol Med Res
Year1982
Volume6
Pages169-205
AuthorsGracy RW
TitleGlucosephosphate and triosephosphate isomerases: significance of isozyme structural differences in evolution, physiology, and aging.
[7]
PubMed ID6838203
JournalArch Biochem Biophys
Year1983
Volume221
Pages489-98
AuthorsPullan LM, Igarashi P, Noltmann EA
TitleArginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by phenylglyoxal and butanedione and in the protection by substrate analogs.
[8]
PubMed ID8381960
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages1237-41
AuthorsSeeholzer SH
TitlePhosphoglucose isomerase: a ketol isomerase with aldol C2-epimerase activity.
[9]
PubMed ID9417984
JournalJ Struct Biol
Year1997
Volume120
Pages196-200
AuthorsHsiao CD, Chou CC, Hsiao YY, Sun YJ, Meng M
TitleExpression, purification, and crystallization of two isozymes of 6-phosphoglucose isomerase of Bacillus stearothermophilus.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID99254054
PubMed ID10318897
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages5412-7
AuthorsSun YJ, Chou CC, Chen WS, Wu RT, Meng M, Hsiao CD
TitleThe crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.
Related PDB2pgi
Related Swiss-protP13376
[11]
PubMed ID10595547
JournalProtein Sci
Year1999
Volume8
Pages2438-43
AuthorsMeng M, Chane TL, Sun YJ, Hsiao CD
TitleProbing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.
[12]
PubMed ID10653639
JournalBiochemistry
Year2000
Volume39
Pages955-64
AuthorsJeffery CJ, Bahnson BJ, Chien W, Ringe D, Petsko GA
TitleCrystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator.
Related PDB1dqr
[13]
PubMed ID10770936
JournalJ Biol Chem
Year2000
Volume275
Pages23154-60
AuthorsChou CC, Sun YJ, Meng M, Hsiao CD
TitleThe crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition.
Related PDB1c7q,1c7r
[14]
PubMed ID11030090
JournalJ Enzyme Inhib
Year2000
Volume15
Pages509-15
AuthorsHardre R, Salmon L, Opperdoes FR
TitleCompetitive inhibition of Trypanosoma brucei phosphoglucose isomerase by D-arabinose-5-phosphate derivatives.
[15]
PubMed ID11327814
JournalBiochemistry
Year2001
Volume40
Pages1560-6
AuthorsJeffery CJ, Hardre R, Salmon L
TitleCrystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis.
Related PDB1g98
[16]
PubMed ID11425306
JournalBiochemistry
Year2001
Volume40
Pages7799-805
AuthorsLee JH, Chang KZ, Patel V, Jeffery CJ
TitleCrystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate.
Related PDB1hox
[17]
PubMed ID11418102
JournalFEBS Lett
Year2001
Volume499
Pages11-4
AuthorsMeng M, Lin HY, Hsieh CJ, Chen YT
TitleFunctions of the conserved anionic amino acids and those interacting with the substrate phosphate group of phosphoglucose isomerase.
[18]
PubMed ID11371164
JournalJ Mol Biol
Year2001
Volume309
Pages447-63
AuthorsRead J, Pearce J, Li X, Muirhead H, Chirgwin J, Davies C
TitleThe crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia.
Related PDB1iat
[19]
PubMed ID12368100
JournalJ Mol Biol
Year2002
Volume323
Pages77-84
AuthorsArsenieva D, Jeffery CJ
TitleConformational changes in phosphoglucose isomerase induced by ligand binding.
Related PDB1hm5
[20]
PubMed ID11983887
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages5872-7
AuthorsArsenieva D, Hardre R, Salmon L, Jeffery CJ
TitleThe crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid.
Related PDB1koj
[21]
PubMed ID12402366
JournalProteins
Year2002
Volume49
Pages577-9
AuthorsDavies C, Muirhead H
TitleCrystal structure of phosphoglucose isomerase from pig muscle and its complex with 5-phosphoarabinonate.
Related PDB1gzd,1gzv
[22]
PubMed ID12054796
JournalJ Mol Biol
Year2002
Volume318
Pages985-97
AuthorsTanaka N, Haga A, Uemura H, Akiyama H, Funasaka T, Nagase H, Raz A, Nakamura KT
TitleInhibition mechanism of cytokine activity of human autocrine motility factor examined by crystal structure analyses and site-directed mutagenesis studies.
Related PDB1iri,1jiq
[23]
PubMed ID12595702
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages453-65
AuthorsDavies C, Muirhead H
TitleStructure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function.
Related PDB1n8t
[24]
PubMed ID12777791
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages1111-3
AuthorsDavies C, Muirhead H, Chirgwin J
TitleThe structure of human phosphoglucose isomerase complexed with a transition-state analogue.
Related PDB1nuh
[25]
PubMed ID12573240
JournalBiochim Biophys Acta
Year2003
Volume1645
Pages117-22
AuthorsCordeiro AT, Godoi PH, Silva CH, Garratt RC, Oliva G, Thiemann OH
TitleCrystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps.
Related PDB1jlh


createdupdated
2004-05-202009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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