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Q09770 (AGM2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable phosphoacetylglucosamine mutase 2

Short name=PAGM
EC=5.4.2.3
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase
Gene names
ORF Names:SPAC1296.01c, SPAC22F3.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

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 – 542542Probable phosphoacetylglucosamine mutase 2
PRO_0000148018

Sites

Active site771Phosphoserine intermediate By similarity
Metal binding771Magnesium; via phosphate group By similarity
Metal binding2921Magnesium By similarity
Metal binding2941Magnesium By similarity
Metal binding2961Magnesium By similarity

Amino acid modifications

Modified residue771Phosphoserine Ref.2
Modified residue821Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q09770 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 131871396737609E

FASTA54258,916
        10         20         30         40         50         60 
MSDAEDSDSI VNEFVTAIVR ESDKFAKVHS YPMQYGTGGY RADAELLSSV AFRTGVIASF 

        70         80         90        100        110        120 
LSAKLHGQPV GLMVTASHNA SSENGLKIVN ILSSLDSSKW EAYLDQVVNA DSADELTVCL 

       130        140        150        160        170        180 
TSILKKAKII PGSEARVFVG YDSRSTSEIL AQAVIDGIVV CKAKYENFGL LTTPQLHYMV 

       190        200        210        220        230        240 
KASQTYGTPD AIGEPTERGY FEKLSKAYQS LMTGKKIKGT VLIDAANGVG AAKIKELAKY 

       250        260        270        280        290        300 
IDPKLFPIEI VNDNIDNPEL LNNSCGADFV RTQQKPPNGI SAPKHARCAS FDGDADRIVY 

       310        320        330        340        350        360 
FAFGSHSFHL LDGDKICALF AQFLIDLIRS TGLDLQVGIV QTAYANGAST AFFQKTLKVP 

       370        380        390        400        410        420 
VLCVSPGLKH LYHAAQAYDV GVFFEANGHG TILVSHAALS KIISHEVLSP AQFNALKTLK 

       430        440        450        460        470        480 
TVFELINQTD GDAITNLLLV EVILAHKNCT LKEWNQLYSE IPSRLIRCEV EDRSIYTTTD 

       490        500        510        520        530        540 
AEQKLVTPEG LQEKIDALVA KYTGGRAFVR SSGTEDAVRV YAEASSRGES EDLALRIVEL 


LH 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA91066.1.
PIRT37562.
S62416. T38190.
RefSeqNP_593040.2. NM_001018439.3.

3D structure databases

ProteinModelPortalQ09770.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280512. 27 interactions.
MINTMINT-4694906.
STRING4896.SPAC1296.01c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1296.01c.1; SPAC1296.01c.1:pep; SPAC1296.01c.
GeneID3361436.
KEGGspo:SPAC1296.01c.

Organism-specific databases

PomBaseSPAC1296.01c.

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000210027.
KOK01836.
OMAHNASSEN.
OrthoDBEOG7V1G0D.
PhylomeDBQ09770.

Enzyme and pathway databases

UniPathwayUPA00113; UER00530.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 1 hit.
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.
IPR016657. PAGM.
[Graphical view]
PANTHERPTHR22573:SF3. PTHR22573:SF3. 1 hit.
PfamPF02878. PGM_PMM_I. 1 hit.
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.
ProtoNetSearch...

Other

NextBio20811483.
PROQ09770.

Entry information

Entry nameAGM2_SCHPO
AccessionPrimary (citable) accession number: Q09770
Secondary accession number(s): O94610
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 29, 2001
Last modified: April 16, 2014
This is version 101 of the entry and version 2 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways