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Reviewed, UniProtKB/Swiss-Prot Q9P4V2 (AGM1_CANAL)

Last modified September 22, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phosphoacetylglucosamine mutase
      Short name=PAGM
    EC=5.4.2.3
Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
Gene names
Name: AGM1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.

Sequence similarities

Belongs to the phosphohexose mutase family.

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Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoacetylglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 544544Phosphoacetylglucosamine mutase
PRO_0000148016

Sites

Active site661Phosphoserine intermediate By similarity
Metal binding661Magnesium; via phosphate group By similarity
Metal binding2901Magnesium By similarity
Metal binding2921Magnesium By similarity
Metal binding2941Magnesium By similarity

Experimental info

Sequence conflict2381K → R in AAF64520. Ref.2
Sequence conflict3081K → N in AAF64520. Ref.2
Sequence conflict3501S → Y in AAF64520. Ref.2

Secondary structure

1 ............................................................................................ 544
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9P4V2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B022662342FA6D58

FASTA54460,478
        10         20         30         40         50         60 
MSIEQTLSQY LPSHPKPQGV TFTYGTAGFR MKADKLDYVT FTVGIIASLR SKYLQGKTVG 

        70         80         90        100        110        120 
VMITASHNPP EDNGVKVVDP LGSMLESSWE KYATDLANAS PSPSNDSEGE KNSLVEVIKN 

       130        140        150        160        170        180 
LVSDLKIDLS IPANVVIARD SRESSPALSM ATIDGFQSVP NTKYQDFGLF TTPELHYVTR 

       190        200        210        220        230        240 
TLNDPDFGKP TEDGYYSKLA KSFQEIYTIC ESNNEKIDIT IDAANGVGAP KIQELLEKYL 

       250        260        270        280        290        300 
HKEISFTVVN GDYKQPNLLN FDCGADYVKT NQKLPKNVKP VNNKLYASFD GDADRLICYY 

       310        320        330        340        350        360 
QNNDNKFKLL DGDKLSTLFA LFLQQLFKQI DPTKISLNIG VVQTAYANGS STKYVEDVLK 

       370        380        390        400        410        420 
IPVRCTPTGV KHLHHEAENF DIGVYFEANG HGTVIFNPEA EKKIFDYKPN NDNEAKAIKV 

       430        440        450        460        470        480 
LQNFSQLINQ TVGDAISDLL AVLIVVHYLK LSPSDWDNEY TDLPNKLVKV IVPDRSIFKT 

       490        500        510        520        530        540 
TNAERTLVEP KGMQDEIDKL VAQYPNGRSF VRASGTEDAV RVYAEADTQN NVEELSKAVS 


ELVK

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References

[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: 11004509] [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].
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB032082 Genomic DNA. Translation: BAB00614.1.
AF253056 Genomic DNA. Translation: AAF64520.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2DKAX-ray1.93A/B1-544[»]
2DKCX-ray2.20A/B1-544[»]
2DKDX-ray2.10A/B1-544[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.4.2.3. 1124.

Family and domain databases

InterProIPR005844. 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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 1 hit.
PfamPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFPIRSF016408. PAGM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAGM1_CANAL
AccessionPrimary (citable) accession number: Q9P4V2
Secondary accession number(s): Q9P8H8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: September 22, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents