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Protein

Glucosamine-6-phosphate deaminase

Gene

nagB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

Enzyme regulationi

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

Pathwayi: N-acetylneuraminate degradation

This protein is involved in step 5 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. N-acetylneuraminate lyase (nanA)
  2. N-acetylmannosamine kinase (nanK)
  3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
  4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
  5. Glucosamine-6-phosphate deaminase (nagB)
This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei72Proton acceptor; for enolization step1 Publication1
Active sitei141For ring-opening step1 Publication1
Active sitei143Proton acceptor; for ring-opening step1 Publication1
Active sitei148For ring-opening step1 Publication1
Sitei151Part of the allosteric site1
Sitei158Part of the allosteric site1
Sitei160Part of the allosteric site1
Sitei161Part of the allosteric site1
Sitei254Part of the allosteric site1

GO - Molecular functioni

  • glucosamine-6-phosphate deaminase activity Source: EcoCyc
  • hydrolase activity Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB-KW
  • N-acetylglucosamine catabolic process Source: EcoCyc
  • N-acetylneuraminate catabolic process Source: EcoCyc
  • 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.
BRENDAi3.5.99.6. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10633. nagB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi118C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi141D → N: Large decrease in activity. 1 Publication1
Mutagenesisi143H → Q: Loss of activity for the deamination reaction but not for the reverse reaction; complete loss of the homotropic cooperativity. 1 Publication1
Mutagenesisi148E → Q: Large decrease in activity. 1 Publication1
Mutagenesisi174F → A: Loss of activity in the absence of the allosteric activator. 1
Mutagenesisi239C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity; decrease in allosteric interaction energy. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001601431 – 266Glucosamine-6-phosphate deaminaseAdd BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi219Interchain1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0A759.
PaxDbiP0A759.
PRIDEiP0A759.

Interactioni

Subunit structurei

Homohexamer; trimer of disulfide-linked dimers.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261792. 7 interactors.
DIPiDIP-35992N.
IntActiP0A759. 11 interactors.
STRINGi511145.b0678.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi9 – 27Combined sources19
Beta strandi31 – 33Combined sources3
Beta strandi35 – 39Combined sources5
Helixi46 – 57Combined sources12
Beta strandi66 – 76Combined sources11
Helixi85 – 92Combined sources8
Helixi94 – 96Combined sources3
Helixi101 – 103Combined sources3
Helixi114 – 128Combined sources15
Beta strandi132 – 136Combined sources5
Beta strandi157 – 161Combined sources5
Helixi164 – 170Combined sources7
Helixi171 – 173Combined sources3
Turni174 – 176Combined sources3
Helixi178 – 180Combined sources3
Beta strandi183 – 187Combined sources5
Helixi190 – 194Combined sources5
Beta strandi199 – 203Combined sources5
Helixi206 – 208Combined sources3
Helixi209 – 217Combined sources9
Beta strandi222 – 224Combined sources3
Helixi225 – 231Combined sources7
Beta strandi233 – 239Combined sources7
Helixi242 – 244Combined sources3
Helixi249 – 263Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A759.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CKA. Bacteria.
COG0363. LUCA.
HOGENOMiHOG000064979.
InParanoidiP0A759.
KOiK02564.
OMAiSALQMHR.
PhylomeDBiP0A759.

Family and domain databases

CDDicd01399. GlcN6P_deaminase. 1 hit.
HAMAPiMF_01241. GlcN6P_deamin. 1 hit.
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

        10         20         30         40         50
MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK
60 70 80 90 100
ALVEMHKAGQ VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP
110 120 130 140 150
AENINLLNGN APDIDAECRQ YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA
160 170 180 190 200
SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ VPKYALTVGV GTLLDAEEVM
210 220 230 240 250
ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD EPSTMELKVK
260
TLRYFNELEA ENIKGL
Length:266
Mass (Da):29,774
Last modified:June 7, 2005 - v1
Checksum:iD1443A40E74AC08E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70N → NM in AAC09324 (PubMed:2190615).Curated1
Sequence conflicti91Missing in AAC09324 (PubMed:2190615).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001237072.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73772; AAC73772; b0678.
BAA35321; BAA35321; BAA35321.
GeneIDi945290.
KEGGiecj:JW0664.
eco:b0678.
PATRICi32116541. VBIEscCol129921_0703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001237072.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261792. 7 interactors.
DIPiDIP-35992N.
IntActiP0A759. 11 interactors.
STRINGi511145.b0678.

Proteomic databases

EPDiP0A759.
PaxDbiP0A759.
PRIDEiP0A759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73772; AAC73772; b0678.
BAA35321; BAA35321; BAA35321.
GeneIDi945290.
KEGGiecj:JW0664.
eco:b0678.
PATRICi32116541. VBIEscCol129921_0703.

Organism-specific databases

EchoBASEiEB0627.
EcoGeneiEG10633. nagB.

Phylogenomic databases

eggNOGiENOG4105CKA. Bacteria.
COG0363. LUCA.
HOGENOMiHOG000064979.
InParanoidiP0A759.
KOiK02564.
OMAiSALQMHR.
PhylomeDBiP0A759.

Enzyme and pathway databases

UniPathwayiUPA00629; UER00684.
BioCyciEcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
ECOL316407:JW0664-MONOMER.
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER.
BRENDAi3.5.99.6. 2026.
SABIO-RKP0A759.

Miscellaneous databases

EvolutionaryTraceiP0A759.
PROiP0A759.

Family and domain databases

CDDicd01399. GlcN6P_deaminase. 1 hit.
HAMAPiMF_01241. GlcN6P_deamin. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 101 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.