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Q09687

- AGM1_SCHPO

UniProt

Q09687 - AGM1_SCHPO

Protein

Probable phosphoacetylglucosamine mutase 1

Gene

SPAC13C5.05c

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 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 sitei51 – 511Phosphoserine intermediateBy similarity
    Metal bindingi51 – 511Magnesium; via phosphate groupBy similarity
    Metal bindingi267 – 2671MagnesiumBy similarity
    Metal bindingi269 – 2691MagnesiumBy similarity
    Metal bindingi271 – 2711MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoacetylglucosamine mutase activity Source: PomBase

    GO - Biological processi

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

    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 1 (EC:5.4.2.3)
    Short name:
    PAGM
    Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
    Gene namesi
    ORF Names:SPAC13C5.05c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC13C5.05c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase
    3. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 518518Probable phosphoacetylglucosamine mutase 1PRO_0000148017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphothreonine1 Publication
    Modified residuei51 – 511Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ09687.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4694067.
    STRINGi4896.SPAC13C5.05c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ09687.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    HOGENOMiHOG000210027.
    KOiK01836.
    OMAiDWETHAT.
    OrthoDBiEOG7V1G0D.
    PhylomeDBiQ09687.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    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.
    IPR016657. PAGM.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 2 hits.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016408. PAGM. 1 hit.
    SUPFAMiSSF53738. SSF53738. 4 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q09687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKNKKYSYG TAGFRTKASD LEAAVYSSGV AAALRSMELK GKTIGVMITA    50
    SHNPVEDNGV KIIDADGGML AMEWEDKCTQ LANAPSKAEF DFLIKQFLTP 100
    TTCQPKVIIG YDTRPSSPRL AELLKVCLDE MSASYIDYGY ITTPQLHWLV 150
    RLINKSTAAS FLEEGPPITE YYDTLTSAFS KIDPSMQDSP TVSRVVVDCA 200
    NGVGSQPLKT VAGLVKDSLS IELVNTDVRA SELLNNGCGA DFVKTKQSPP 250
    LALEGKIKPN QLYASIDGDA DRLIFYYINQ NRKFHLLDGD KISTALVGYL 300
    NILVKKSGMP FSLGVVQTAY ANGASTEYLQ DLGITTVFTP TGVKHLHKAA 350
    KEFDIGVYFE ANGHGTVLFS DKALANLAHP FFTPSPVQAA AIEQLQSYSV 400
    LINQAIGDAI SDLLATISVL NALHWDASAW SNTYKDLPNK LAKVKVSDRT 450
    IYKSTDAERR LVSPDGLQEK IDALVAKYEK GRSFVRASGT EDVVRVYAEA 500
    STKQAADELC EKVCQLVL 518
    Length:518
    Mass (Da):56,347
    Last modified:November 1, 1995 - v1
    Checksum:iDA8ACB0008C29594
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA90456.1.
    PIRiS59642.
    RefSeqiNP_592933.1. NM_001018334.2.

    Genome annotation databases

    EnsemblFungiiSPAC13C5.05c.1; SPAC13C5.05c.1:pep; SPAC13C5.05c.
    GeneIDi2542320.
    KEGGispo:SPAC13C5.05c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA90456.1 .
    PIRi S59642.
    RefSeqi NP_592933.1. NM_001018334.2.

    3D structure databases

    ProteinModelPortali Q09687.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4694067.
    STRINGi 4896.SPAC13C5.05c-1.

    Proteomic databases

    MaxQBi Q09687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC13C5.05c.1 ; SPAC13C5.05c.1:pep ; SPAC13C5.05c .
    GeneIDi 2542320.
    KEGGi spo:SPAC13C5.05c.

    Organism-specific databases

    PomBasei SPAC13C5.05c.

    Phylogenomic databases

    eggNOGi COG1109.
    HOGENOMi HOG000210027.
    KOi K01836.
    OMAi DWETHAT.
    OrthoDBi EOG7V1G0D.
    PhylomeDBi Q09687.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 20803381.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    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.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR016657. PAGM.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 2 hits.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016408. PAGM. 1 hit.
    SUPFAMi SSF53738. SSF53738. 4 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    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 THR-49 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiAGM1_SCHPO
    AccessioniPrimary (citable) accession number: Q09687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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