UniProtKB - P0A759 (NAGB_ECOLI)
Protein
Glucosamine-6-phosphate deaminase
Gene
nagB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Miscellaneous
Disulfide bonds seem not to be essential for the stability of the oligomer under physiological conditions.
Catalytic activityi
- EC:3.5.99.6
Activity regulationi
Allosterically activated by N-acetylglucosamine 6-phosphate (GlcNAc6P). Competitively inhibited by 2-amino-2-deoxy-D-glucitol-6-phosphate (GlcN-ol-6P).
: N-acetylneuraminate degradation Pathwayi
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:
- N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA)
- N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK)
- Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE), Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
- N-acetylglucosamine-6-phosphate deacetylase (nagA)
- Glucosamine-6-phosphate deaminase (nagB), Glucosamine-6-phosphate deaminase (nagB)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 72 | Proton acceptor; for enolization step1 Publication | 1 | |
Active sitei | 141 | For ring-opening step1 Publication | 1 | |
Active sitei | 143 | Proton acceptor; for ring-opening step1 Publication | 1 | |
Active sitei | 148 | For ring-opening step1 Publication | 1 | |
Sitei | 151 | Part of the allosteric site | 1 | |
Sitei | 158 | Part of the allosteric site | 1 | |
Sitei | 160 | Part of the allosteric site | 1 | |
Sitei | 161 | Part of the allosteric site | 1 | |
Sitei | 254 | Part of the allosteric site | 1 |
GO - Molecular functioni
- glucosamine-6-phosphate deaminase activity Source: EcoCyc
- identical protein binding Source: EcoCyc
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB-KW
- glucosamine catabolic process Source: GO_Central
- N-acetylglucosamine catabolic process Source: EcoCyc
- N-acetylneuraminate catabolic process Source: EcoCyc
- UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Allosteric enzyme, Hydrolase |
Biological process | Carbohydrate metabolism |
Enzyme and pathway databases
BioCyci | EcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER |
BRENDAi | 3.5.99.6, 2026 |
SABIO-RKi | P0A759 |
UniPathwayi | UPA00629;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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 118 | C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 141 | D → N: Large decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 143 | H → Q: Loss of activity for the deamination reaction but not for the reverse reaction; complete loss of the homotropic cooperativity. 1 Publication | 1 | |
Mutagenesisi | 148 | E → Q: Large decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 174 | F → A: Loss of activity in the absence of the allosteric activator. | 1 | |
Mutagenesisi | 239 | C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity; decrease in allosteric interaction energy. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB02445, 2-Deoxy-2-Amino Glucitol-6-Phosphate DB03951, N-acetyl-D-glucosamine-6-phosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000160143 | 1 – 266 | Glucosamine-6-phosphate deaminaseAdd BLAST | 266 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 219 | Interchain1 Publication |
Keywords - PTMi
Disulfide bondProteomic databases
jPOSTi | P0A759 |
PaxDbi | P0A759 |
PRIDEi | P0A759 |
Interactioni
Subunit structurei
Homohexamer; trimer of disulfide-linked dimers.
1 PublicationGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4261792, 32 interactors |
DIPi | DIP-35992N |
IntActi | P0A759, 11 interactors |
STRINGi | 511145.b0678 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A759 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A759 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0363, Bacteria |
HOGENOMi | CLU_049611_0_1_6 |
InParanoidi | P0A759 |
PhylomeDBi | P0A759 |
Family and domain databases
CDDi | cd01399, GlcN6P_deaminase, 1 hit |
HAMAPi | MF_01241, GlcN6P_deamin, 1 hit |
InterProi | View protein in InterPro IPR006148, Glc/Gal-6P_isomerase IPR004547, Glucosamine6P_isomerase IPR018321, Glucosamine6P_isomerase_CS IPR037171, NagB/RpiA_transferase-like |
PANTHERi | PTHR11280, PTHR11280, 1 hit |
Pfami | View protein in Pfam PF01182, Glucosamine_iso, 1 hit |
SUPFAMi | SSF100950, SSF100950, 1 hit |
TIGRFAMsi | TIGR00502, nagB, 1 hit |
PROSITEi | View protein in PROSITE PS01161, GLC_GALNAC_ISOMERASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A759-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 70 | N → NM in AAC09324 (PubMed:2190615).Curated | 1 | |
Sequence conflicti | 91 | Missing in AAC09324 (PubMed:2190615).Curated | 1 |
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 |
PIRi | A29895, MUECNG |
RefSeqi | NP_415204.1, NC_000913.3 WP_001237072.1, NZ_STEB01000044.1 |
Genome annotation databases
EnsemblBacteriai | AAC73772; AAC73772; b0678 BAA35321; BAA35321; BAA35321 |
GeneIDi | 58461678 945290 |
KEGGi | ecj:JW0664 eco:b0678 |
PATRICi | fig|1411691.4.peg.1600 |
Similar proteinsi
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 |
PIRi | A29895, MUECNG |
RefSeqi | NP_415204.1, NC_000913.3 WP_001237072.1, NZ_STEB01000044.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P0A759 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261792, 32 interactors |
DIPi | DIP-35992N |
IntActi | P0A759, 11 interactors |
STRINGi | 511145.b0678 |
Chemistry databases
DrugBanki | DB02445, 2-Deoxy-2-Amino Glucitol-6-Phosphate DB03951, N-acetyl-D-glucosamine-6-phosphate |
Proteomic databases
jPOSTi | P0A759 |
PaxDbi | P0A759 |
PRIDEi | P0A759 |
Genome annotation databases
EnsemblBacteriai | AAC73772; AAC73772; b0678 BAA35321; BAA35321; BAA35321 |
GeneIDi | 58461678 945290 |
KEGGi | ecj:JW0664 eco:b0678 |
PATRICi | fig|1411691.4.peg.1600 |
Organism-specific databases
EchoBASEi | EB0627 |
Phylogenomic databases
eggNOGi | COG0363, Bacteria |
HOGENOMi | CLU_049611_0_1_6 |
InParanoidi | P0A759 |
PhylomeDBi | P0A759 |
Enzyme and pathway databases
UniPathwayi | UPA00629;UER00684 |
BioCyci | EcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER |
BRENDAi | 3.5.99.6, 2026 |
SABIO-RKi | P0A759 |
Miscellaneous databases
EvolutionaryTracei | P0A759 |
PROi | PR:P0A759 |
Family and domain databases
CDDi | cd01399, GlcN6P_deaminase, 1 hit |
HAMAPi | MF_01241, GlcN6P_deamin, 1 hit |
InterProi | View protein in InterPro IPR006148, Glc/Gal-6P_isomerase IPR004547, Glucosamine6P_isomerase IPR018321, Glucosamine6P_isomerase_CS IPR037171, NagB/RpiA_transferase-like |
PANTHERi | PTHR11280, PTHR11280, 1 hit |
Pfami | View protein in Pfam PF01182, Glucosamine_iso, 1 hit |
SUPFAMi | SSF100950, SSF100950, 1 hit |
TIGRFAMsi | TIGR00502, nagB, 1 hit |
PROSITEi | View protein in PROSITE PS01161, GLC_GALNAC_ISOMERASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NAGB_ECOLI | |
Accessioni | P0A759Primary (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: | April 7, 2021 | |
This is version 130 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families