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P0A759

- NAGB_ECOLI

UniProt

P0A759 - NAGB_ECOLI

Protein

Glucosamine-6-phosphate deaminase

Gene

nagB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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

    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

    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 deaminasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701N → NM in AAC09324. (PubMed:2190615)Curated
    Sequence conflicti91 – 911Missing in AAC09324. (PubMed:2190615)Curated

    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

    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: October 1, 2014
    This is version 86 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