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P0A759 (NAGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucosamine-6-phosphate deaminase

EC=3.5.99.6
Alternative name(s):
GlcN6P deaminase
Short name=GNPDA
Glucosamine-6-phosphate isomerase
Gene names
Name:nagB
Synonyms:glmD
Ordered Locus Names:b0678, JW0664
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. HAMAP-Rule MF_01241

Catalytic activity

Alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3. HAMAP-Rule MF_01241

Enzyme regulation

Allosterically activated by N-acetylglucosamine 6-phosphate (GlcNAc6P). Competitively inhibited by 2-amino-2-deoxy-D-glucitol-6-phosphate (GlcN-ol-6P). HAMAP-Rule MF_01241

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5. HAMAP-Rule MF_01241

Subunit structure

Homohexamer; trimer of disulfide-linked dimers. Ref.7

Miscellaneous

Disulfide bonds seem not to be essential for the stability of the oligomer under physiological conditions.

Sequence similarities

Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Glucosamine-6-phosphate deaminase HAMAP-Rule MF_01241
PRO_0000160143

Sites

Active site721Proton acceptor; for enolization step Ref.8
Active site1411For ring-opening step Ref.8
Active site1431Proton acceptor; for ring-opening step Ref.8
Active site1481For ring-opening step Ref.8
Site1511Part of the allosteric site
Site1581Part of the allosteric site
Site1601Part of the allosteric site
Site1611Part of the allosteric site
Site2541Part of the allosteric site

Amino acid modifications

Disulfide bond219Interchain Ref.7

Experimental info

Mutagenesis1181C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity. Ref.6
Mutagenesis1411D → N: Large decrease in activity. Ref.8
Mutagenesis1431H → Q: Loss of activity for the deamination reaction but not for the reverse reaction; complete loss of the homotropic cooperativity. Ref.8
Mutagenesis1481E → Q: Large decrease in activity. Ref.8
Mutagenesis1741F → A: Loss of activity in the absence of the allosteric activator.
Mutagenesis2391C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity; decrease in allosteric interaction energy. Ref.6
Sequence conflict701N → NM in AAC09324. Ref.2
Sequence conflict911Missing in AAC09324. Ref.2

Secondary structure

................................................. 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A759 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: D1443A40E74AC08E

FASTA26629,774
        10         20         30         40         50         60 
MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK ALVEMHKAGQ 

        70         80         90        100        110        120 
VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP AENINLLNGN APDIDAECRQ 

       130        140        150        160        170        180 
YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ 

       190        200        210        220        230        240 
VPKYALTVGV GTLLDAEEVM ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD 

       250        260 
EPSTMELKVK TLRYFNELEA ENIKGL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase."
Rogers M.J., Ohgi T., Plumbridge J., Soell D.
Gene 62:197-207(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli."
Peri K.G., Goldie H., Waygood E.B.
Biochem. Cell Biol. 68:123-137(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"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."
Altamirano M.M., Plumbridge J.A., Calcagno M.L.
Biochemistry 31:1153-1158(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-118 AND CYS-239.
[7]"Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides."
Altamirano M.M., Plumbridge J.A., Barba H.A., Calcagno M.L.
Biochem. J. 295:645-648(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[8]"On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase."
Montero-Moran G.M., Lara-Gonzalez S., Alvarez-Anorve L.I., Plumbridge J.A., Calcagno M.L.
Biochemistry 40:10187-10196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES, MUTAGENESIS OF ASP-141; HIS-143 AND GLU-148.
[9]"Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1-A resolution."
Oliva G., Fontes M.R.M., Garratt R.C., Altamirano M.M., Calcagno M.L., Horjales E.
Structure 3:1323-1332(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH THE INHIBITOR 2-AMINO-2-DEOXY-D-GLUCITOL-6-PHOSPHATE.
[10]"The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3-A resolution."
Horjales E., Altamirano M.M., Calcagno M.L., Garratt R.C., Oliva G.
Structure 7:527-537(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[11]"Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase."
Rudino-Pinera E., Morales-Arrieta S., Rojas-Trejo S.P., Horjales E.
Acta Crystallogr. D 58:10-20(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH FRUCTOSE-6-PHOSPHATE AND N-ACETYLGLUCOSAMINE-6-PHOSPHATE.
[12]"On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase."
Bustos-Jaimes I., Sosa-Peinado A., Rudino-Pinera E., Horjales E., Calcagno M.L.
J. Mol. Biol. 319:183-189(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF MUTANT ALA-174.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19284 Genomic DNA. Translation: AAA24191.1.
AF052007 Genomic DNA. Translation: AAC09324.1.
U00096 Genomic DNA. Translation: AAC73772.1.
AP009048 Genomic DNA. Translation: BAA35321.1.
PIRMUECNG. A29895.
RefSeqNP_415204.1. NC_000913.3.
YP_488958.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CD5X-ray2.30A1-266[»]
1DEAX-ray2.10A/B1-266[»]
1FQOX-ray2.20A/B1-266[»]
1FRZX-ray2.20A/B1-266[»]
1FS5X-ray1.73A/B1-266[»]
1FS6X-ray2.20A1-266[»]
1FSFX-ray1.90A1-266[»]
1HORX-ray2.40A/B1-266[»]
1HOTX-ray2.40A/B1-266[»]
1JT9X-ray2.06A1-266[»]
2WU1X-ray2.20A/B1-266[»]
ProteinModelPortalP0A759.
SMRP0A759. Positions 1-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35992N.
IntActP0A759. 11 interactions.
STRING511145.b0678.

Proteomic databases

PaxDbP0A759.
PRIDEP0A759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73772; AAC73772; b0678.
BAA35321; BAA35321; BAA35321.
GeneID12932798.
945290.
KEGGecj:Y75_p0657.
eco:b0678.
PATRIC32116541. VBIEscCol129921_0703.

Organism-specific databases

EchoBASEEB0627.
EcoGeneEG10633. nagB.

Phylogenomic databases

eggNOGCOG0363.
HOGENOMHOG000064979.
KOK02564.
OMAYFREMEA.
OrthoDBEOG6WX4S3.
PhylomeDBP0A759.

Enzyme and pathway databases

BioCycEcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
ECOL316407:JW0664-MONOMER.
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
SABIO-RKP0A759.
UniPathwayUPA00629; UER00684.

Gene expression databases

GenevestigatorP0A759.

Family and domain databases

HAMAPMF_01241. GlcN6P_deamin.
InterProIPR006148. Glc/Gal-6P_isomerase.
IPR004547. Glucosamine6P_isomerase.
IPR018321. Glucosamine6P_isomerase_CS.
[Graphical view]
PANTHERPTHR11280. PTHR11280. 1 hit.
PfamPF01182. Glucosamine_iso. 1 hit.
[Graphical view]
TIGRFAMsTIGR00502. nagB. 1 hit.
PROSITEPS01161. GLC_GALNAC_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A759.
PROP0A759.

Entry information

Entry nameNAGB_ECOLI
AccessionPrimary (citable) accession number: P0A759
Secondary accession number(s): O68603, P09375
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene