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
47987
16134
61553
PubChem 22247451
962
440997
222
439160
1cd5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1deaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1deaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1horA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1horB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1hotA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1hotB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fqoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:FPC
1fqoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:FPC
1frzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1frzB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fs5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fs5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fs6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fsfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jt9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ne7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1ne7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1ne7C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1ne7D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1ne7E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:AGP Unbound Unbound
1ne7F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1deaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1deaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1horA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1horB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1hotA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1hotB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1fqoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1fqoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1frzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1frzB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1fs5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1fs5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1fs6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1fsfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1jt9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1ne7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1ne7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1ne7C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1ne7D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1ne7E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 72;ASP 141;HIS 143;GLU 148
1ne7F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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