DB code: S00367

CATH domain 3.40.50.1360 : Rossmann fold Catalytic domain
E.C. 3.5.99.6
CSA 1cd5
M-CSA 1cd5
MACiE M0060

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P46926 Glucosamine-6-phosphate isomerase 1
EC 3.5.99.6
Glucosamine-6-phosphate deaminase 1
GlcN6P deaminase 1
GNPDA 1
Oscillin
NP_005462.1 (Protein)
NM_005471.4 (DNA/RNA sequence)
PF01182 (Glucosamine_iso)
[Graphical View]
P0A759 Glucosamine-6-phosphate deaminase
EC 3.5.99.6
Glucosamine-6-phosphate isomerase
GlcN6P deaminase
GNPDA
NP_415204.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488958.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01182 (Glucosamine_iso)
[Graphical View]

KEGG enzyme name
glucosamine-6-phosphate deaminase
glucosaminephosphate isomerase
glucosamine-6-phosphate isomerase
phosphoglucosaminisomerase
glucosamine phosphate deaminase
aminodeoxyglucosephosphate isomerase
phosphoglucosamine isomerase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P46926 GNPI1_HUMAN D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). Homohexamer. Cytoplasm (By similarity).
P0A759 NAGB_ECOLI D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). Homohexamer, trimer of disulfide-linked dimers.

KEGG Pathways
Map code Pathways E.C.
MAP00530 Aminosugars metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00001 C00352 C00014 C00085
E.C.
Compound H2O D-Glucosamine 6-phosphate NH3 D-Fructose 6-phosphate
Type H2O amine group,carbohydrate,phosphate group/phosphate ion amine group,organic ion carbohydrate,phosphate group/phosphate ion
ChEBI 15377
 15377
 		47987
 47987
 		16134
 16134
 		61553
 61553
PubChem 22247451
 962
 22247451
 962
 		440997
 440997
 		222
 222
 		439160
 439160
1cd5A Unbound Unbound Unbound
1deaA Unbound Unbound Unbound
1deaB Unbound Unbound Unbound
1horA Bound:AGP Unbound Unbound
1horB Bound:AGP Unbound Unbound
1hotA Unbound Unbound Unbound
1hotB Unbound Unbound Unbound
1fqoA Unbound Unbound Bound:FPC
1fqoB Unbound Unbound Bound:FPC
1frzA Unbound Unbound Unbound
1frzB Unbound Unbound Unbound
1fs5A Unbound Unbound Unbound
1fs5B Unbound Unbound Unbound
1fs6A Unbound Unbound Unbound
1fsfA Unbound Unbound Unbound
1jt9A Unbound Unbound Unbound
1ne7A Bound:AGP Unbound Unbound
1ne7B Bound:AGP Unbound Unbound
1ne7C Bound:AGP Unbound Unbound
1ne7D Bound:AGP Unbound Unbound
1ne7E Bound:AGP Unbound Unbound
1ne7F Bound:AGP Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot P0A759, P46926 & literature [7], [9]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cd5A ASP 72;ASP 141;HIS 143;GLU 148
1deaA ASP 72;ASP 141;HIS 143;GLU 148
1deaB ASP 72;ASP 141;HIS 143;GLU 148
1horA ASP 72;ASP 141;HIS 143;GLU 148
1horB ASP 72;ASP 141;HIS 143;GLU 148
1hotA ASP 72;ASP 141;HIS 143;GLU 148
1hotB ASP 72;ASP 141;HIS 143;GLU 148
1fqoA ASP 72;ASP 141;HIS 143;GLU 148
1fqoB ASP 72;ASP 141;HIS 143;GLU 148
1frzA ASP 72;ASP 141;HIS 143;GLU 148
1frzB ASP 72;ASP 141;HIS 143;GLU 148
1fs5A ASP 72;ASP 141;HIS 143;GLU 148
1fs5B ASP 72;ASP 141;HIS 143;GLU 148
1fs6A ASP 72;ASP 141;HIS 143;GLU 148
1fsfA ASP 72;ASP 141;HIS 143;GLU 148
1jt9A ASP 72;ASP 141;HIS 143;GLU 148
1ne7A ASP 72;ASP 141;HIS 143;GLU 148
1ne7B ASP 72;ASP 141;HIS 143;GLU 148
1ne7C ASP 72;ASP 141;HIS 143;GLU 148
1ne7D ASP 72;ASP 141;HIS 143;GLU 148
1ne7E ASP 72;ASP 141;HIS 143;GLU 148
1ne7F ASP 72;ASP 141;HIS 143;GLU 148

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[7]
Fig.5, p.1329-1330 7
[10]
p.222
[12]
Fig.1, p.10194-10196 7

References
[1]
Resource
Comments
Medline ID
PubMed ID 2821923
Journal Arch Biochem Biophys
Year 1987
Volume 258
Pages 95-100
Authors Altamirano MM, Mulliert G, Calcagno M
Title Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2111170
Journal Biochim Biophys Acta
Year 1990
Volume 1038
Pages 291-4
Authors Altamirano MM, Calcagno M
Title Zinc binding and its trapping by allosteric transition in glucosamine-6-phosphate deaminase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments MUTAGENESIS OF CYS-118 AND CYS-239.
Medline ID 92135199
PubMed ID 1734962
Journal Biochemistry
Year 1992
Volume 31
Pages 1153-8
Authors Altamirano MM, Plumbridge JA, Calcagno ML
Title Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis.
Related PDB
Related UniProtKB P0A759
[4]
Resource
Comments
Medline ID
PubMed ID 1518057
Journal J Mol Biol
Year 1992
Volume 226
Pages 1283-6
Authors Horjales E, Altamirano MM, Calcagno ML, Dauter Z, Wilson K, Garratt RC, Oliva G
Title Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12.
Related PDB
Related UniProtKB
[5]
Resource
Comments DISULFIDE BONDS.
Medline ID 94059012
PubMed ID 8240271
Journal Biochem J
Year 1993
Volume 295
Pages 645-8
Authors Altamirano MM, Plumbridge JA, Barba HA, Calcagno ML
Title Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides.
Related PDB
Related UniProtKB P0A759
[6]
Resource
Comments
Medline ID
PubMed ID 8125098
Journal Eur J Biochem
Year 1994
Volume 220
Pages 409-13
Authors Altamirano MM, Hernandez-Arana A, Tello-Solis S, Calcagno ML
Title Spectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH THE INHIBITOR 2-AMINO-2-DEOXY-D-GLUCITOL-6-PHOSPHATE.
Medline ID 96363670
PubMed ID 8747459
Journal Structure
Year 1995
Volume 3
Pages 1323-32
Authors Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E
Title Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.
Related PDB 1dea 1hor 1hot
Related UniProtKB P0A759
[8]
Resource
Comments
Medline ID
PubMed ID 9601045
Journal Biochemistry
Year 1998
Volume 37
Pages 7844-9
Authors Montero-Moran GM, Horjales E, Calcagno ML, Altamirano MM
Title Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 99306035
PubMed ID 10378272
Journal Structure Fold Des
Year 1999
Volume 7
Pages 527-37
Authors Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G
Title The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution.
Related PDB 1cd5
Related UniProtKB P0A759
[10]
Resource
Comments
Medline ID
PubMed ID 10926504
Journal J Mol Biol
Year 2000
Volume 301
Pages 219-27
Authors Lara-Gonzalez S, Dixon HB, Mendoza-Hernandez G, Altamirano MM, Calcagno ML
Title On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11594728
Journal Arch Biochem Biophys
Year 2001
Volume 394
Pages 156-60
Authors Bustos-Jaimes I, Calcagno ML
Title Allosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli.
Related PDB
Related UniProtKB
[12]
Resource
Comments ACTIVE SITES, AND MUTAGENESIS OF ASP-141; HIS-143 AND GLU-148.
Medline ID 21404989
PubMed ID 11513596
Journal Biochemistry
Year 2001
Volume 40
Pages 10187-96
Authors Montero-Moran GM, Lara-Gonzalez S, Alvarez-Anorve LI, Plumbridge JA, Calcagno ML
Title On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase.
Related PDB
Related UniProtKB P0A759
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH FRUCTOSE-6-PHOSPHATE AND N-ACETYLGLUCOSAMINE-6-PHOSPHATE.
Medline ID 21620768
PubMed ID 11752775
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 10-20
Authors Rudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E
Title Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
Related PDB 1fqo 1frz 1fs5 1fs6 1fsf
Related UniProtKB P0A759
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF MUTANT F174A.
Medline ID 22047883
PubMed ID 12051945
Journal J Mol Biol
Year 2002
Volume 319
Pages 183-9
Authors Bustos-Jaimes I, Sosa-Peinado A, Rudino-Pinera E, Horjales E, Calcagno ML
Title On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase.
Related PDB 1jt9
Related UniProtKB P0A759
[15]
Resource
Comments
Medline ID
PubMed ID 12965206
Journal FEBS Lett
Year 2003
Volume 551
Pages 63-70
Authors Arreola R, Valderrama B, Morante ML, Horjales E
Title Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 14678787
Journal Arch Biochem Biophys
Year 2004
Volume 421
Pages 77-84
Authors Cisneros DA, Montero-Moran GM, Lara-Gonzalez S, Calcagno ML
Title Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements.
Related PDB
Related UniProtKB

Comments
Although this enzyme is classified into hydrolases, it does not catalyzes ordinary "hydrolysis" reaction.
According to the literature [7] & [12], this enzyme catalyzes the following reactions.
(A) Isomerization (open ring), or Elimination of hydroxyl group accompanied by double-bond formation
(B) Isomerization (change in the position of double-bond), to form Schiff-base (adlimine),
(C) Schiff-base dehydration,
(D) Isomerization (close ring), or addition to double-bond.

Created Updated
2004-08-13 2009-02-26