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Q9P4V2 (AGM1_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P4V2 [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] [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032082 Genomic DNA. Translation: BAB00614.1.
AF253056 Genomic DNA. Translation: AAF64520.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKAX-ray1.93A/B1-544[»]
2DKCX-ray2.20A/B1-544[»]
2DKDX-ray2.10A/B1-544[»]
ProteinModelPortalQ9P4V2.
SMRQ9P4V2. Positions 1-544.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1109.

Enzyme and pathway databases

BRENDA5.4.2.3. 1096.
UniPathwayUPA00113; UER00530.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
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]
PfamPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFPIRSF016408. PAGM. 1 hit.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9P4V2.

Entry information

Entry nameAGM1_CANAX
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: June 11, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways