Entry Information
Protein Name GlmM
Accession No P31120
Protein description Phosphoglucosamine mutase
pI/Mw (Da)
Theoretical Experimental
5.71/47412.38 -
Protein function and expression Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Reference(s) Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

Swiss-Prot Database Reference

Entry information
Entry Name GLMM_ECOLI
Primary accession number P31120
Secondary accession numbers Q2M936 
Integrated into Swiss-Prot on 1993-07-01
Sequence was last modified on 2004-03-01 (Sequence version 2)
Annotations were last modified on 2006-06-13 (Entry version 56)
Name and origin of the protein
Protein name Phosphoglucosamine mutase
Synonyms EC 5.4.2.10 Phosphoglucosamine mutase
Gene name Name : glmM
OrderedLocusName : b3176
SynonymName : mrsA
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
PubMed=8244950[NCBI, ExPASy, EBI, Israel, Japan]
Dallas W.S. , Dev I.K. , Ray P.H. ,
"The dihydropteroate synthase gene, folP, is near the leucine tRNA gene, leuU, on the Escherichia coli chromosome."
J. Bacteriol.175:7743-7744(1993) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12

Wang R. , Kushner S.R. ,
Submitted (1993-09) to the EMBL/GenBank/DDBJ databases 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
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. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[5] PROTEIN SEQUENCE OF 1-11, AND CHARACTERIZATION.DOI=10.1074/jbc.271.1.32;PubMed=8550580[NCBI, ExPASy, EBI, Israel, Japan]
Mengin-Lecreulx D. , van Heijenoort J. ,
"Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli."
J. Biol. Chem.271:32-39(1996) 
[6] ACTIVE SITE SER-101.DOI=10.1128/JB.182.5.1280-1285.2000;PubMed=10671448[NCBI, ExPASy, EBI, Israel, Japan]
Jolly L. , Pompeo F. , van Heijenoort J. , Fassy F. , Mengin-Lecreulx D. ,
"Autophosphorylation of phosphoglucosamine mutase from Escherichia coli."
J. Bacteriol.182:1280-1285(2000) 
Comments
  • FUNCTION : Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
  • CATALYTIC ACTIVITY : Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
  • COFACTOR : Binds 1 magnesium ion per subunit (By similarity)
  • SIMILARITY : Belongs to the phosphohexose mutase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL L12968;AAA16122.1;-;Unassigned_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U01376;AAA97510.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U18997;AAA57977.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC76208.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAE77220.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR I41215;I41215.
    3D structure databases
    ModBase P31120
    Protein-protein interaction databases
    IntAct P31120;-.
    DIP P31120
    Enzyme and pathway databases
    BioCyc EcoCyc:PHOSGLUCOSAMINEMUT-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB1514;-.
    EcoGene EG11553;glmM.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    HAMAP MF_01554-;1.
    PBIL [Family/Alignment/Tree]
    InterPro IPR006352;GlmM.
    IPR005841;PG/PMM_mutase.
    IPR005844;PG_PMM_ABAI.
    IPR005845;PG_PMM_ABAII.
    IPR005846;PG_PMM_ABAIII.
    IPR005843;PG_PMM_C.
    Graphical view of domain structure
    Pfam PF02878;PGM_PMM_I;1.
    PF02879;PGM_PMM_II;1.
    PF02880;PGM_PMM_III;1.
    PF00408;PGM_PMM_IV;1.
    Pfam graphical view of domain structure
    PRINTS PR00509;PGMPMM.
    TIGRFAMs TIGR01455;glmM;1.
    BLOCKS P31120
    PROSITE PS00710;PGM_PMM;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b3176.
    Other
    ProtoNet P31120
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; Direct protein sequencing; Isomerase; Magnesium; Metal-binding; Phosphorylation;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    INIT_MET    0     0      
    CHAIN    1   444    444  Phosphoglucosamine mutase  PRO_0000147887
    ACT_SITE  101   101    Phosphoserine intermediate  
    METAL  101   101    Magnesium (via phosphate group)(by similarity)  
    METAL  240   240    Magnesium(by similarity)  
    METAL  242   242    Magnesium(by similarity)  
    METAL  244   244    Magnesium(by similarity)  
    CONFLICT   68    68    A -> R: (in Ref. 2)  
    CONFLICT  161   161    C -> S: (in Ref. 2)  
    CONFLICT  166   166    P -> R: (in Ref. 2)  
    CONFLICT  177   180    VVDC -> LVIG: (in Ref. 2)  
    CONFLICT  410   410    R -> C: (in Ref. 2)  
    CONFLICT  416   416    P -> R: (in Ref. 2)  
    Sequence information
    Length: 444AA [This is the length of the unprocessed precursor] Molecular weight: 47412Da [This is the MW of the unprocessed precursor] CRC64: 02BE974B93BB7AB5[This is a checksum on the sequence]
            10         20         30         40         50         60
    SNRKYFGTDG IRGRVGDAPI TPDFVLKLGW AAGKVLARHG SRKIIIGKDT RISGYMLESA
            70         80         90        100        110        120
    LEAGLAAAGL SALFTGPMPT PAVAYLTRTF RAEAGIVISA SHNPFYDNGI KFFSIDGTKL
           130        140        150        160        170        180
    PDAVEEAIEA EMEKEISCVD SAELGKASRI VDAAGRYIEF CKATFPNELS LSELKIVVDC
           190        200        210        220        230        240
    ANGATYHIAP NVLRELGANV IAIGCEPNGV NINAEVGATD VRALQARVLA EKADLGIAFD
           250        260        270        280        290        300
    GDGDRVIMVD HEGNKVDGDQ IMYIIAREGL RQGQLRGGAV GTLMSNMGLE LALKQLGIPF
           310        320        330        340        350        360
    ARAKVGDRYV LEKMQEKGWR IGAENSGHVI LLDKTTTGDG IVAGLQVLAA MARNHMSLHD
           370        380        390        400        410        420
    LCSGMKMFPQ ILVNVRYTAG SGDPLEHESV KAVTAEVEAA LGNRGRVLLR KSGTEPLIRV
           430        440 
    MVEGEDEAQV TEFAHRIADA VKAV
    P31120 in FASTA format