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Q09770

- AGM2_SCHPO

UniProt

Q09770 - AGM2_SCHPO

Protein

Probable phosphoacetylglucosamine mutase 2

Gene

SPAC1296.01c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (29 Aug 2001)
      Previous versions | rss
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    Functioni

    Interconverts GlcNAc-6-P and GlcNAc-1-P.By similarity

    Catalytic activityi

    N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei77 – 771Phosphoserine intermediateBy similarity
    Metal bindingi77 – 771Magnesium; via phosphate groupBy similarity
    Metal bindingi292 – 2921MagnesiumBy similarity
    Metal bindingi294 – 2941MagnesiumBy similarity
    Metal bindingi296 – 2961MagnesiumBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoacetylglucosamine mutase activity Source: PomBase

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. UDP-N-acetylglucosamine biosynthetic process Source: PomBase

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_188592. Synthesis of UDP-N-acetyl-glucosamine.
    UniPathwayiUPA00113; UER00530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable phosphoacetylglucosamine mutase 2 (EC:5.4.2.3)
    Short name:
    PAGM
    Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
    Gene namesi
    ORF Names:SPAC1296.01c, SPAC22F3.01
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC1296.01c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. mannosyltransferase complex Source: PomBase
    3. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Probable phosphoacetylglucosamine mutase 2PRO_0000148018Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphoserine1 Publication
    Modified residuei82 – 821Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ09770.

    Interactioni

    Protein-protein interaction databases

    BioGridi280512. 27 interactions.
    MINTiMINT-4694906.
    STRINGi4896.SPAC1296.01c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ09770.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    HOGENOMiHOG000210027.
    KOiK01836.
    OMAiVANERCA.
    OrthoDBiEOG7V1G0D.
    PhylomeDBiQ09770.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 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.
    IPR005843. A-D-PHexomutase_C.
    IPR016657. PAGM.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016408. PAGM. 1 hit.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q09770-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDAEDSDSI VNEFVTAIVR ESDKFAKVHS YPMQYGTGGY RADAELLSSV    50
    AFRTGVIASF LSAKLHGQPV GLMVTASHNA SSENGLKIVN ILSSLDSSKW 100
    EAYLDQVVNA DSADELTVCL TSILKKAKII PGSEARVFVG YDSRSTSEIL 150
    AQAVIDGIVV CKAKYENFGL LTTPQLHYMV KASQTYGTPD AIGEPTERGY 200
    FEKLSKAYQS LMTGKKIKGT VLIDAANGVG AAKIKELAKY IDPKLFPIEI 250
    VNDNIDNPEL LNNSCGADFV RTQQKPPNGI SAPKHARCAS FDGDADRIVY 300
    FAFGSHSFHL LDGDKICALF AQFLIDLIRS TGLDLQVGIV QTAYANGAST 350
    AFFQKTLKVP VLCVSPGLKH LYHAAQAYDV GVFFEANGHG TILVSHAALS 400
    KIISHEVLSP AQFNALKTLK TVFELINQTD GDAITNLLLV EVILAHKNCT 450
    LKEWNQLYSE IPSRLIRCEV EDRSIYTTTD AEQKLVTPEG LQEKIDALVA 500
    KYTGGRAFVR SSGTEDAVRV YAEASSRGES EDLALRIVEL LH 542
    Length:542
    Mass (Da):58,916
    Last modified:August 29, 2001 - v2
    Checksum:i131871396737609E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA91066.1.
    PIRiT37562.
    T38190. S62416.
    RefSeqiNP_593040.2. NM_001018439.3.

    Genome annotation databases

    EnsemblFungiiSPAC1296.01c.1; SPAC1296.01c.1:pep; SPAC1296.01c.
    GeneIDi3361436.
    KEGGispo:SPAC1296.01c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA91066.1 .
    PIRi T37562.
    T38190. S62416.
    RefSeqi NP_593040.2. NM_001018439.3.

    3D structure databases

    ProteinModelPortali Q09770.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 280512. 27 interactions.
    MINTi MINT-4694906.
    STRINGi 4896.SPAC1296.01c-1.

    Proteomic databases

    MaxQBi Q09770.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC1296.01c.1 ; SPAC1296.01c.1:pep ; SPAC1296.01c .
    GeneIDi 3361436.
    KEGGi spo:SPAC1296.01c.

    Organism-specific databases

    PomBasei SPAC1296.01c.

    Phylogenomic databases

    eggNOGi COG1109.
    HOGENOMi HOG000210027.
    KOi K01836.
    OMAi VANERCA.
    OrthoDBi EOG7V1G0D.
    PhylomeDBi Q09770.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00530 .
    Reactomei REACT_188592. Synthesis of UDP-N-acetyl-glucosamine.

    Miscellaneous databases

    NextBioi 20811483.
    PROi Q09770.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 1 hit.
    InterProi IPR005844. 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.
    IPR005843. A-D-PHexomutase_C.
    IPR016657. PAGM.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016408. PAGM. 1 hit.
    SUPFAMi SSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiAGM2_SCHPO
    AccessioniPrimary (citable) accession number: Q09770
    Secondary accession number(s): O94610
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3