Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P57750

- AGM1_ARATH

UniProt

P57750 - AGM1_ARATH

Protein

Phosphoacetylglucosamine mutase

Gene

DRT101

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (24 Jan 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei68 – 681Phosphoserine intermediateBy similarity
    Metal bindingi68 – 681Magnesium; via phosphate groupBy similarity
    Metal bindingi286 – 2861MagnesiumBy similarity
    Metal bindingi288 – 2881MagnesiumBy similarity
    Metal bindingi290 – 2901MagnesiumBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoacetylglucosamine mutase activity Source: RefGenome
    3. phosphoglucomutase activity Source: RefGenome

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glucose 1-phosphate metabolic process Source: RefGenome
    3. photoreactive repair Source: TAIR
    4. response to UV Source: TAIR
    5. UDP-N-acetylglucosamine biosynthetic process Source: RefGenome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G18070-MONOMER.
    ReactomeiREACT_190863. 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
    DNA-damage-repair/toleration protein DRT101
    N-acetylglucosamine-phosphate mutase
    Gene namesi
    Name:DRT101
    Ordered Locus Names:At5g18070
    ORF Names:MRG7.2
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G18070.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. mitochondrion Source: TAIR
    3. plasmodesma Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556Phosphoacetylglucosamine mutasePRO_0000148015Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP57750.
    PRIDEiP57750.

    Expressioni

    Gene expression databases

    GenevestigatoriP57750.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G18070.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliP57750.
    SMRiP57750. Positions 19-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    HOGENOMiHOG000210027.
    InParanoidiP57750.
    KOiK01836.
    OMAiDIVRVYA.
    PhylomeDBiP57750.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 2 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.
    IPR016657. PAGM.
    [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]
    PIRSFiPIRSF016408. PAGM. 1 hit.
    SUPFAMiSSF53738. SSF53738. 4 hits.
    SSF55957. SSF55957. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P57750-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEIQIASIL KSSELFPIPQ GVKLSYGTAG FRGDAKLLES TVYRVGILSA    50
    LRSLKLGSAT VGLMITASHN KVSDNGIKVS DPSGFMLSQE WEPFADQIAN 100
    ASSPEELVSL IRKFMEKEEI AIGENNKGAE VWLGRDTRPS GESLLRAGEI 150
    GVGSILGSVA IDIGILTTPQ LHWMVRAKNK GLKATENDYF ENLSTSFRCL 200
    IDLIPSSGND KLEISKLLVD GANGVGGQKI EKLRGSLSNL DVEIRNTGRD 250
    GGVLNEGVGA DFVQKEKVLP VGFGFKDVGM RCASLDGDAD RLVYFYIPSD 300
    SSEKVELLDG DKILSLFALF IKEQLNALED DEERKQSRLG VVQTAYANGA 350
    STDYLKHLGL DVVFAKTGVK HLHEKAAEFD IGIYFEANGH GTILFSESFL 400
    SWLVSKQKDL TAKGQGGSEE HKAVSRLMAV SNLINQAVGD ALSGVLLVEV 450
    ILQHLGWSIE KWNELYKDLP SRQIKVEVPD RTAVVTTSEE TEALRPMGIQ 500
    DAINSEIKKY SRGRAFIRPS GTEDVVRVYA EASTQEDADS LANSVAQLVK 550
    SFLGSS 556
    Length:556
    Mass (Da):60,391
    Last modified:January 24, 2001 - v1
    Checksum:iBCADE44F14DDC3D0
    GO

    Sequence cautioni

    The sequence AAA72352.1 differs from that shown. Reason: Sequencing errors.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012246 Genomic DNA. Translation: BAB09465.1.
    CP002688 Genomic DNA. Translation: AED92503.1.
    AY075620 mRNA. Translation: AAL91631.1.
    L11367 mRNA. Translation: AAA72352.1. Sequence problems.
    PIRiS35270.
    RefSeqiNP_568359.2. NM_121812.2.
    UniGeneiAt.466.

    Genome annotation databases

    EnsemblPlantsiAT5G18070.1; AT5G18070.1; AT5G18070.
    GeneIDi831926.
    KEGGiath:AT5G18070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012246 Genomic DNA. Translation: BAB09465.1 .
    CP002688 Genomic DNA. Translation: AED92503.1 .
    AY075620 mRNA. Translation: AAL91631.1 .
    L11367 mRNA. Translation: AAA72352.1 . Sequence problems.
    PIRi S35270.
    RefSeqi NP_568359.2. NM_121812.2.
    UniGenei At.466.

    3D structure databases

    ProteinModelPortali P57750.
    SMRi P57750. Positions 19-554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G18070.1-P.

    Proteomic databases

    PaxDbi P57750.
    PRIDEi P57750.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G18070.1 ; AT5G18070.1 ; AT5G18070 .
    GeneIDi 831926.
    KEGGi ath:AT5G18070.

    Organism-specific databases

    TAIRi AT5G18070.

    Phylogenomic databases

    eggNOGi COG1109.
    HOGENOMi HOG000210027.
    InParanoidi P57750.
    KOi K01836.
    OMAi DIVRVYA.
    PhylomeDBi P57750.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00530 .
    BioCyci ARA:AT5G18070-MONOMER.
    Reactomei REACT_190863. Synthesis of UDP-N-acetyl-glucosamine.

    Miscellaneous databases

    PROi P57750.

    Gene expression databases

    Genevestigatori P57750.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 2 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.
    IPR016657. PAGM.
    [Graphical view ]
    Pfami PF02878. 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 ]
    PIRSFi PIRSF016408. PAGM. 1 hit.
    SUPFAMi SSF53738. SSF53738. 4 hits.
    SSF55957. SSF55957. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
      Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
      DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Selection of Arabidopsis cDNAs that partially correct phenotypes of Escherichia coli DNA-damage-sensitive mutants and analysis of two plant cDNAs that appear to express UV-specific dark repair activities."
      Pang Q., Hays J.B., Rajagopal I., Schaefer T.S.
      Plant Mol. Biol. 22:411-426(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-556.
      Strain: cv. Columbia.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.

    Entry informationi

    Entry nameiAGM1_ARATH
    AccessioniPrimary (citable) accession number: P57750
    Secondary accession number(s): Q05211
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3