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Q9P4V2

- AGM1_CANAX

UniProt

Q9P4V2 - AGM1_CANAX

Protein

Phosphoacetylglucosamine mutase

Gene

AGM1

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

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

    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 sitei66 – 661Phosphoserine intermediateBy similarity
    Metal bindingi66 – 661Magnesium; via phosphate groupBy similarity
    Metal bindingi290 – 2901MagnesiumBy similarity
    Metal bindingi292 – 2921MagnesiumBy similarity
    Metal bindingi294 – 2941MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoacetylglucosamine mutase activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi5.4.2.3. 1096.
    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
    Gene namesi
    Name:AGM1
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 544544Phosphoacetylglucosamine mutasePRO_0000148016Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Structurei

    Secondary structure

    1
    544
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 86
    Helixi11 – 133
    Beta strandi28 – 325
    Helixi33 – 353
    Helixi37 – 5317
    Turni54 – 563
    Beta strandi58 – 636
    Beta strandi72 – 787
    Beta strandi82 – 843
    Helixi87 – 893
    Helixi90 – 989
    Beta strandi99 – 1013
    Helixi114 – 12411
    Beta strandi133 – 1397
    Helixi145 – 15713
    Beta strandi159 – 16911
    Helixi172 – 18312
    Helixi185 – 1873
    Helixi192 – 20716
    Beta strandi217 – 2226
    Helixi228 – 23912
    Turni241 – 2433
    Beta strandi244 – 2507
    Helixi256 – 2583
    Turni259 – 2624
    Helixi265 – 2717
    Beta strandi286 – 2894
    Beta strandi296 – 3016
    Beta strandi307 – 3104
    Helixi312 – 32716
    Turni332 – 3343
    Beta strandi339 – 3435
    Helixi349 – 3579
    Beta strandi363 – 3653
    Helixi370 – 3778
    Beta strandi380 – 3867
    Beta strandi392 – 3965
    Helixi398 – 4069
    Helixi412 – 42716
    Beta strandi430 – 4323
    Helixi435 – 44814
    Helixi453 – 4575
    Beta strandi465 – 4706
    Helixi475 – 4773
    Beta strandi479 – 4813
    Turni482 – 4843
    Beta strandi486 – 4905
    Helixi493 – 5019
    Beta strandi508 – 5136
    Beta strandi520 – 5256
    Helixi529 – 54315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DKAX-ray1.93A/B1-544[»]
    2DKCX-ray2.20A/B1-544[»]
    2DKDX-ray2.10A/B1-544[»]
    ProteinModelPortaliQ9P4V2.
    SMRiQ9P4V2. Positions 1-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P4V2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.

    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. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9P4V2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIEQTLSQY LPSHPKPQGV TFTYGTAGFR MKADKLDYVT FTVGIIASLR    50
    SKYLQGKTVG VMITASHNPP EDNGVKVVDP LGSMLESSWE KYATDLANAS 100
    PSPSNDSEGE KNSLVEVIKN LVSDLKIDLS IPANVVIARD SRESSPALSM 150
    ATIDGFQSVP NTKYQDFGLF TTPELHYVTR TLNDPDFGKP TEDGYYSKLA 200
    KSFQEIYTIC ESNNEKIDIT IDAANGVGAP KIQELLEKYL HKEISFTVVN 250
    GDYKQPNLLN FDCGADYVKT NQKLPKNVKP VNNKLYASFD GDADRLICYY 300
    QNNDNKFKLL DGDKLSTLFA LFLQQLFKQI DPTKISLNIG VVQTAYANGS 350
    STKYVEDVLK IPVRCTPTGV KHLHHEAENF DIGVYFEANG HGTVIFNPEA 400
    EKKIFDYKPN NDNEAKAIKV LQNFSQLINQ TVGDAISDLL AVLIVVHYLK 450
    LSPSDWDNEY TDLPNKLVKV IVPDRSIFKT TNAERTLVEP KGMQDEIDKL 500
    VAQYPNGRSF VRASGTEDAV RVYAEADTQN NVEELSKAVS ELVK 544
    Length:544
    Mass (Da):60,478
    Last modified:October 1, 2000 - v1
    Checksum:iB022662342FA6D58
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381K → R in AAF64520. 1 PublicationCurated
    Sequence conflicti308 – 3081K → N in AAF64520. 1 PublicationCurated
    Sequence conflicti350 – 3501S → Y in AAF64520. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032082 Genomic DNA. Translation: BAB00614.1.
    AF253056 Genomic DNA. Translation: AAF64520.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032082 Genomic DNA. Translation: BAB00614.1 .
    AF253056 Genomic DNA. Translation: AAF64520.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DKA X-ray 1.93 A/B 1-544 [» ]
    2DKC X-ray 2.20 A/B 1-544 [» ]
    2DKD X-ray 2.10 A/B 1-544 [» ]
    ProteinModelPortali Q9P4V2.
    SMRi Q9P4V2. Positions 1-544.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1109.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00530 .
    BRENDAi 5.4.2.3. 1096.

    Miscellaneous databases

    EvolutionaryTracei Q9P4V2.

    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. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis."
      Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.
      Biochim. Biophys. Acta 1492:369-376(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Identification and isolation of Candida albicans AGM1."
      Spettel C., Eschrich D., Koetter P., Entian K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiAGM1_CANAX
    AccessioniPrimary (citable) accession number: Q9P4V2
    Secondary accession number(s): Q9P8H8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 72 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

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3