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Q9CYR6

- AGM1_MOUSE

UniProt

Q9CYR6 - AGM1_MOUSE

Protein

Phosphoacetylglucosamine mutase

Gene

Pgm3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Jun 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 sitei64 – 641Phosphoserine intermediateBy similarity
    Metal bindingi64 – 641Magnesium; via phosphate groupBy similarity
    Metal bindingi276 – 2761MagnesiumBy similarity
    Metal bindingi278 – 2781MagnesiumBy similarity
    Metal bindingi280 – 2801MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoacetylglucosamine mutase activity Source: MGI
    3. phosphoglucomutase activity Source: MGI

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glucose 1-phosphate metabolic process Source: MGI
    3. hemopoiesis Source: MGI
    4. spermatogenesis Source: MGI
    5. UDP-N-acetylglucosamine biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198714. Synthesis of UDP-N-acetyl-glucosamine.
    UniPathwayiUPA00113; UER00530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoacetylglucosamine mutase (EC:5.4.2.3)
    Short name:
    PAGM
    Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
    Phosphoglucomutase-3
    Short name:
    PGM 3
    Gene namesi
    Name:Pgm3
    Synonyms:Agm1, Pgm-3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:97566. Pgm3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Phosphoacetylglucosamine mutasePRO_0000148014Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei64 – 641PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CYR6.
    PaxDbiQ9CYR6.
    PRIDEiQ9CYR6.

    PTM databases

    PhosphoSiteiQ9CYR6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CYR6.
    BgeeiQ9CYR6.
    CleanExiMM_PGM3.
    GenevestigatoriQ9CYR6.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000070871.

    Structurei

    Secondary structure

    1
    542
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi449 – 4546
    Beta strandi459 – 4624
    Beta strandi470 – 4745
    Helixi477 – 48711
    Beta strandi488 – 4969
    Beta strandi498 – 51215
    Helixi513 – 53018

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WJWNMR-A442-540[»]
    ProteinModelPortaliQ9CYR6.
    SMRiQ9CYR6. Positions 4-541.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CYR6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    GeneTreeiENSGT00390000000509.
    HOVERGENiHBG024321.
    InParanoidiB2RS40.
    KOiK01836.
    OMAiDIVRVYA.
    OrthoDBiEOG7W6WKJ.
    PhylomeDBiQ9CYR6.
    TreeFamiTF105670.

    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.
    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.
    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.

    Q9CYR6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLEAVCKRS ALHAKPQGLI LQYGTAGFRT NAQHLDHIMF RMGLLAVLRS    50
    KQTRSTIGVM VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLASAEEQ 100
    DVRQVLAAIV EKEAVDLTQT AFVVIARDTR PSSEKLSQSV IDGVTVLGGQ 150
    FHDYGLLTTP QLHYMVYCRN SGGRYGQATV EGYCQKLSKA FVDLTNQVSC 200
    SGDVKRSVKV DCANGIGALK LREMEHYFSR GLSVLLFNDG TQGRLNHLCG 250
    ADFVKSQQKP PQGIEMKSGE RCCSFDGDAD RIVYYYCDAD GHFHLIDGDK 300
    IATLISSFLK ELLLEIGESV NLGVVQTAYA NGSSTRYLEE VMKVPVYCTK 350
    TGVKHLHHKA QEFDIGVYFE ANGHGTALFS EAVEVKIKRL AQELDDGKGK 400
    AARTLASIID LFNQAAGDAI SDMLVIEAIL ALKGLTVQQW DAIYVDLPNR 450
    QLKVKVADRR VISTTDAERQ AVTPPGLQEA INDLVKKYTL ARAFVRPSGT 500
    EDIVRVYAEA NSQESADRLA YEVSLLVFQL AGGIGERPQP TF 542
    Length:542
    Mass (Da):59,453
    Last modified:June 1, 2001 - v1
    Checksum:iB00E3D0F38BE4090
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK013402 mRNA. Translation: BAB28834.1.
    AK028066 mRNA. Translation: BAC25733.1.
    AK049337 mRNA. Translation: BAC33692.1.
    AK051706 mRNA. Translation: BAC34728.1.
    AK160913 mRNA. Translation: BAE36087.1.
    AK165513 mRNA. Translation: BAE38229.1.
    AK169082 mRNA. Translation: BAE40866.1.
    AK169787 mRNA. Translation: BAE41366.1.
    BC138700 mRNA. Translation: AAI38701.1.
    CCDSiCCDS23381.1.
    RefSeqiNP_001157218.1. NM_001163746.1.
    NP_082628.3. NM_028352.4.
    UniGeneiMm.390201.

    Genome annotation databases

    EnsembliENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.
    GeneIDi109785.
    KEGGimmu:109785.
    UCSCiuc009qxm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK013402 mRNA. Translation: BAB28834.1 .
    AK028066 mRNA. Translation: BAC25733.1 .
    AK049337 mRNA. Translation: BAC33692.1 .
    AK051706 mRNA. Translation: BAC34728.1 .
    AK160913 mRNA. Translation: BAE36087.1 .
    AK165513 mRNA. Translation: BAE38229.1 .
    AK169082 mRNA. Translation: BAE40866.1 .
    AK169787 mRNA. Translation: BAE41366.1 .
    BC138700 mRNA. Translation: AAI38701.1 .
    CCDSi CCDS23381.1.
    RefSeqi NP_001157218.1. NM_001163746.1.
    NP_082628.3. NM_028352.4.
    UniGenei Mm.390201.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WJW NMR - A 442-540 [» ]
    ProteinModelPortali Q9CYR6.
    SMRi Q9CYR6. Positions 4-541.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000070871.

    PTM databases

    PhosphoSitei Q9CYR6.

    Proteomic databases

    MaxQBi Q9CYR6.
    PaxDbi Q9CYR6.
    PRIDEi Q9CYR6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070064 ; ENSMUSP00000070871 ; ENSMUSG00000056131 .
    GeneIDi 109785.
    KEGGi mmu:109785.
    UCSCi uc009qxm.2. mouse.

    Organism-specific databases

    CTDi 5238.
    MGIi MGI:97566. Pgm3.

    Phylogenomic databases

    eggNOGi COG1109.
    GeneTreei ENSGT00390000000509.
    HOVERGENi HBG024321.
    InParanoidi B2RS40.
    KOi K01836.
    OMAi DIVRVYA.
    OrthoDBi EOG7W6WKJ.
    PhylomeDBi Q9CYR6.
    TreeFami TF105670.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00530 .
    Reactomei REACT_198714. Synthesis of UDP-N-acetyl-glucosamine.

    Miscellaneous databases

    EvolutionaryTracei Q9CYR6.
    NextBioi 362755.
    PROi Q9CYR6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CYR6.
    Bgeei Q9CYR6.
    CleanExi MM_PGM3.
    Genevestigatori Q9CYR6.

    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.
    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.
    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 transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Cerebellum, Embryo, Heart, Kidney, Placenta, Spinal ganglion and Thymus.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "Solution structure of the C-terminal domain of mouse phosphoacetylglucosamine mutase (PAGM)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 442-540.

    Entry informationi

    Entry nameiAGM1_MOUSE
    AccessioniPrimary (citable) accession number: Q9CYR6
    Secondary accession number(s): B2RS40, Q543F9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    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