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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate.1 Publication

Catalytic activityi

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

Autophosphorylation is inhibited by inorganic phosphate or EDTA.1 Publication

Kineticsi

  1. KM=0.05 mM for glucosamine-6-P2 Publications
  2. KM=0.08 mM for glucosamine-1,6-diP2 Publications
  3. KM=0.5 mM for glucose-1,6-diP2 Publications
  4. KM=0.65 mM for glucose-1-P2 Publications
  5. KM=0.06 mM for ATP2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei102 – 1021Phosphoserine intermediate1 Publication
    Metal bindingi102 – 1021Magnesium; via phosphate groupBy similarity
    Metal bindingi241 – 2411MagnesiumBy similarity
    Metal bindingi243 – 2431MagnesiumBy similarity
    Metal bindingi245 – 2451MagnesiumBy similarity

    GO - Molecular functioni

    • magnesium ion binding Source: UniProtKB-HAMAP
    • phosphoglucosamine mutase activity Source: EcoCyc

    GO - Biological processi

    • carbohydrate metabolic process Source: InterPro
    • protein autophosphorylation Source: EcoCyc
    • UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PHOSGLUCOSAMINEMUT-MONOMER.
    ECOL316407:JW3143-MONOMER.
    MetaCyc:PHOSGLUCOSAMINEMUT-MONOMER.
    SABIO-RKP31120.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglucosamine mutase (EC:5.4.2.10)
    Gene namesi
    Name:glmM
    Synonyms:mrsA, yhbF
    Ordered Locus Names:b3176, JW3143
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11553. glmM.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001S → A: 2% of wild-type activity. 1 Publication
    Mutagenesisi100 – 1001S → T: 20-fold increase in the non-specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated). 1 Publication
    Mutagenesisi102 – 1021S → A: Loss of activity in the absence or presence of glucosamine-1,6-diP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 445444Phosphoglucosamine mutasePRO_0000147887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021Phosphoserine; by autocatalysis2 Publications

    Post-translational modificationi

    Activated by phosphorylation. Can autophosphorylate in vitro using ATP, alpha-D-glucosamine 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiP31120.
    PaxDbiP31120.
    PRIDEiP31120.

    PTM databases

    iPTMnetiP31120.

    Interactioni

    Protein-protein interaction databases

    BioGridi4263256. 205 interactions.
    DIPiDIP-10260N.
    IntActiP31120. 15 interactions.
    STRINGi511145.b3176.

    Structurei

    3D structure databases

    ProteinModelPortaliP31120.
    SMRiP31120. Positions 5-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiENOG4107QJF. Bacteria.
    COG1109. LUCA.
    HOGENOMiHOG000268678.
    InParanoidiP31120.
    KOiK03431.
    OMAiNSHCDGR.
    PhylomeDBiP31120.

    Family and domain databases

    CDDicd05802. GlmM. 1 hit.
    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    HAMAPiMF_01554_B. GlmM_B. 1 hit.
    InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    IPR006352. GlmM_bact.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    TIGRFAMsiTIGR01455. glmM. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31120-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD
    60 70 80 90 100
    TRISGYMLES ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS
    110 120 130 140 150
    ASHNPFYDNG IKFFSIDGTK LPDAVEEAIE AEMEKEISCV DSAELGKASR
    160 170 180 190 200
    IVDAAGRYIE FCKATFPNEL SLSELKIVVD CANGATYHIA PNVLRELGAN
    210 220 230 240 250
    VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF DGDGDRVIMV
    260 270 280 290 300
    DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP
    310 320 330 340 350
    FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA
    360 370 380 390 400
    AMARNHMSLH DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA
    410 420 430 440
    ALGNRGRVLL RKSGTEPLIR VMVEGEDEAQ VTEFAHRIAD AVKAV
    Length:445
    Mass (Da):47,544
    Last modified:January 23, 2007 - v3
    Checksum:iECDF9A0378A980EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691A → R in AAA97510 (Ref. 2) Curated
    Sequence conflicti162 – 1621C → S in AAA97510 (Ref. 2) Curated
    Sequence conflicti167 – 1671P → R in AAA97510 (Ref. 2) Curated
    Sequence conflicti178 – 1814VVDC → LVIG in AAA97510 (Ref. 2) Curated
    Sequence conflicti411 – 4111R → C in AAA97510 (Ref. 2) Curated
    Sequence conflicti417 – 4171P → R in AAA97510 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L12968 Unassigned DNA. Translation: AAA16122.1.
    U01376 Genomic DNA. Translation: AAA97510.1.
    U18997 Genomic DNA. Translation: AAA57977.1.
    U00096 Genomic DNA. Translation: AAC76208.1.
    AP009048 Genomic DNA. Translation: BAE77220.1.
    PIRiI41215.
    RefSeqiNP_417643.1. NC_000913.3.
    WP_000071134.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76208; AAC76208; b3176.
    BAE77220; BAE77220; BAE77220.
    GeneIDi947692.
    KEGGiecj:JW3143.
    eco:b3176.
    PATRICi32121770. VBIEscCol129921_3269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L12968 Unassigned DNA. Translation: AAA16122.1.
    U01376 Genomic DNA. Translation: AAA97510.1.
    U18997 Genomic DNA. Translation: AAA57977.1.
    U00096 Genomic DNA. Translation: AAC76208.1.
    AP009048 Genomic DNA. Translation: BAE77220.1.
    PIRiI41215.
    RefSeqiNP_417643.1. NC_000913.3.
    WP_000071134.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP31120.
    SMRiP31120. Positions 5-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263256. 205 interactions.
    DIPiDIP-10260N.
    IntActiP31120. 15 interactions.
    STRINGi511145.b3176.

    PTM databases

    iPTMnetiP31120.

    Proteomic databases

    EPDiP31120.
    PaxDbiP31120.
    PRIDEiP31120.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76208; AAC76208; b3176.
    BAE77220; BAE77220; BAE77220.
    GeneIDi947692.
    KEGGiecj:JW3143.
    eco:b3176.
    PATRICi32121770. VBIEscCol129921_3269.

    Organism-specific databases

    EchoBASEiEB1514.
    EcoGeneiEG11553. glmM.

    Phylogenomic databases

    eggNOGiENOG4107QJF. Bacteria.
    COG1109. LUCA.
    HOGENOMiHOG000268678.
    InParanoidiP31120.
    KOiK03431.
    OMAiNSHCDGR.
    PhylomeDBiP31120.

    Enzyme and pathway databases

    BioCyciEcoCyc:PHOSGLUCOSAMINEMUT-MONOMER.
    ECOL316407:JW3143-MONOMER.
    MetaCyc:PHOSGLUCOSAMINEMUT-MONOMER.
    SABIO-RKP31120.

    Miscellaneous databases

    PROiP31120.

    Family and domain databases

    CDDicd05802. GlmM. 1 hit.
    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    HAMAPiMF_01554_B. GlmM_B. 1 hit.
    InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    IPR006352. GlmM_bact.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    TIGRFAMsiTIGR01455. glmM. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGLMM_ECOLI
    AccessioniPrimary (citable) accession number: P31120
    Secondary accession number(s): Q2M936
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism, with alpha-D-glucosamine 1,6-bisphosphate as an intermediate.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. 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.