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P0A759

- NAGB_ECOLI

UniProt

P0A759 - NAGB_ECOLI

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Protein

Glucosamine-6-phosphate deaminase

Gene
nagB, glmD, b0678, JW0664
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3.UniRule annotation

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Proton acceptor; for enolization step1 Publication
Active sitei141 – 1411For ring-opening step1 Publication
Active sitei143 – 1431Proton acceptor; for ring-opening step1 Publication
Active sitei148 – 1481For ring-opening step1 Publication
Sitei151 – 1511Part of the allosteric site
Sitei158 – 1581Part of the allosteric site
Sitei160 – 1601Part of the allosteric site
Sitei161 – 1611Part of the allosteric site
Sitei254 – 2541Part of the allosteric site

GO - Molecular functioni

  1. glucosamine-6-phosphate deaminase activity Source: EcoCyc
  2. hydrolase activity Source: UniProtKB-KW
  3. identical protein binding Source: EcoCyc

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. N-acetylglucosamine catabolic process Source: EcoCyc
  3. N-acetylneuraminate catabolic process Source: EcoCyc
  4. UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciEcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
ECOL316407:JW0664-MONOMER.
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
SABIO-RKP0A759.
UniPathwayiUPA00629; UER00684.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosamine-6-phosphate deaminase (EC:3.5.99.6)
Alternative name(s):
GlcN6P deaminase
Short name:
GNPDA
Glucosamine-6-phosphate isomerase
Gene namesi
Name:nagB
Synonyms:glmD
Ordered Locus Names:b0678, JW0664
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10633. nagB.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi118 – 1181C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity. 1 Publication
Mutagenesisi141 – 1411D → N: Large decrease in activity. 1 Publication
Mutagenesisi143 – 1431H → Q: Loss of activity for the deamination reaction but not for the reverse reaction; complete loss of the homotropic cooperativity. 1 Publication
Mutagenesisi148 – 1481E → Q: Large decrease in activity. 1 Publication
Mutagenesisi174 – 1741F → A: Loss of activity in the absence of the allosteric activator.
Mutagenesisi239 – 2391C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity; decrease in allosteric interaction energy. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Glucosamine-6-phosphate deaminaseUniRule annotationPRO_0000160143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi219 – 219Interchain1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0A759.
PRIDEiP0A759.

Expressioni

Gene expression databases

GenevestigatoriP0A759.

Interactioni

Subunit structurei

Homohexamer; trimer of disulfide-linked dimers.1 Publication

Protein-protein interaction databases

DIPiDIP-35992N.
IntActiP0A759. 11 interactions.
STRINGi511145.b0678.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54
Helixi9 – 2719
Beta strandi31 – 333
Beta strandi35 – 395
Helixi46 – 5712
Beta strandi66 – 7611
Helixi85 – 928
Helixi94 – 963
Helixi101 – 1033
Helixi114 – 12815
Beta strandi132 – 1365
Beta strandi157 – 1615
Helixi164 – 1707
Helixi171 – 1733
Turni174 – 1763
Helixi178 – 1803
Beta strandi183 – 1875
Helixi190 – 1945
Beta strandi199 – 2035
Helixi206 – 2083
Helixi209 – 2179
Beta strandi222 – 2243
Helixi225 – 2317
Beta strandi233 – 2397
Helixi242 – 2443
Helixi249 – 26315

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A759.
SMRiP0A759. Positions 1-266.

Miscellaneous databases

EvolutionaryTraceiP0A759.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0363.
HOGENOMiHOG000064979.
KOiK02564.
OMAiYFREMEA.
OrthoDBiEOG6WX4S3.
PhylomeDBiP0A759.

Family and domain databases

HAMAPiMF_01241. GlcN6P_deamin.
InterProiIPR006148. Glc/Gal-6P_isomerase.
IPR004547. Glucosamine6P_isomerase.
IPR018321. Glucosamine6P_isomerase_CS.
[Graphical view]
PANTHERiPTHR11280. PTHR11280. 1 hit.
PfamiPF01182. Glucosamine_iso. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00502. nagB. 1 hit.
PROSITEiPS01161. GLC_GALNAC_ISOMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A759-1 [UniParc]FASTAAdd to Basket

« Hide

MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK    50
ALVEMHKAGQ VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP 100
AENINLLNGN APDIDAECRQ YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA 150
SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ VPKYALTVGV GTLLDAEEVM 200
ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD EPSTMELKVK 250
TLRYFNELEA ENIKGL 266
Length:266
Mass (Da):29,774
Last modified:June 7, 2005 - v1
Checksum:iD1443A40E74AC08E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701N → NM in AAC09324. 1 Publication
Sequence conflicti91 – 911Missing in AAC09324. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19284 Genomic DNA. Translation: AAA24191.1.
AF052007 Genomic DNA. Translation: AAC09324.1.
U00096 Genomic DNA. Translation: AAC73772.1.
AP009048 Genomic DNA. Translation: BAA35321.1.
PIRiA29895. MUECNG.
RefSeqiNP_415204.1. NC_000913.3.
YP_488958.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73772; AAC73772; b0678.
BAA35321; BAA35321; BAA35321.
GeneIDi12932798.
945290.
KEGGiecj:Y75_p0657.
eco:b0678.
PATRICi32116541. VBIEscCol129921_0703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19284 Genomic DNA. Translation: AAA24191.1 .
AF052007 Genomic DNA. Translation: AAC09324.1 .
U00096 Genomic DNA. Translation: AAC73772.1 .
AP009048 Genomic DNA. Translation: BAA35321.1 .
PIRi A29895. MUECNG.
RefSeqi NP_415204.1. NC_000913.3.
YP_488958.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CD5 X-ray 2.30 A 1-266 [» ]
1DEA X-ray 2.10 A/B 1-266 [» ]
1FQO X-ray 2.20 A/B 1-266 [» ]
1FRZ X-ray 2.20 A/B 1-266 [» ]
1FS5 X-ray 1.73 A/B 1-266 [» ]
1FS6 X-ray 2.20 A 1-266 [» ]
1FSF X-ray 1.90 A 1-266 [» ]
1HOR X-ray 2.40 A/B 1-266 [» ]
1HOT X-ray 2.40 A/B 1-266 [» ]
1JT9 X-ray 2.06 A 1-266 [» ]
2WU1 X-ray 2.20 A/B 1-266 [» ]
ProteinModelPortali P0A759.
SMRi P0A759. Positions 1-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35992N.
IntActi P0A759. 11 interactions.
STRINGi 511145.b0678.

Proteomic databases

PaxDbi P0A759.
PRIDEi P0A759.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73772 ; AAC73772 ; b0678 .
BAA35321 ; BAA35321 ; BAA35321 .
GeneIDi 12932798.
945290.
KEGGi ecj:Y75_p0657.
eco:b0678.
PATRICi 32116541. VBIEscCol129921_0703.

Organism-specific databases

EchoBASEi EB0627.
EcoGenei EG10633. nagB.

Phylogenomic databases

eggNOGi COG0363.
HOGENOMi HOG000064979.
KOi K02564.
OMAi YFREMEA.
OrthoDBi EOG6WX4S3.
PhylomeDBi P0A759.

Enzyme and pathway databases

UniPathwayi UPA00629 ; UER00684 .
BioCyci EcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
ECOL316407:JW0664-MONOMER.
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
SABIO-RK P0A759.

Miscellaneous databases

EvolutionaryTracei P0A759.
PROi P0A759.

Gene expression databases

Genevestigatori P0A759.

Family and domain databases

HAMAPi MF_01241. GlcN6P_deamin.
InterProi IPR006148. Glc/Gal-6P_isomerase.
IPR004547. Glucosamine6P_isomerase.
IPR018321. Glucosamine6P_isomerase_CS.
[Graphical view ]
PANTHERi PTHR11280. PTHR11280. 1 hit.
Pfami PF01182. Glucosamine_iso. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00502. nagB. 1 hit.
PROSITEi PS01161. GLC_GALNAC_ISOMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiNAGB_ECOLI
AccessioniPrimary (citable) accession number: P0A759
Secondary accession number(s): O68603, P09375
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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