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Q09687 (AGM1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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 1

Short name=PAGM
EC=5.4.2.3
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase
Gene names
ORF Names:SPAC13C5.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length518 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 – 518518Probable phosphoacetylglucosamine mutase 1
PRO_0000148017

Sites

Active site511Phosphoserine intermediate By similarity
Metal binding511Magnesium; via phosphate group By similarity
Metal binding2671Magnesium By similarity
Metal binding2691Magnesium By similarity
Metal binding2711Magnesium By similarity

Amino acid modifications

Modified residue491Phosphothreonine Ref.2
Modified residue511Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q09687 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DA8ACB0008C29594

FASTA51856,347
        10         20         30         40         50         60 
MTKNKKYSYG TAGFRTKASD LEAAVYSSGV AAALRSMELK GKTIGVMITA SHNPVEDNGV 

        70         80         90        100        110        120 
KIIDADGGML AMEWEDKCTQ LANAPSKAEF DFLIKQFLTP TTCQPKVIIG YDTRPSSPRL 

       130        140        150        160        170        180 
AELLKVCLDE MSASYIDYGY ITTPQLHWLV RLINKSTAAS FLEEGPPITE YYDTLTSAFS 

       190        200        210        220        230        240 
KIDPSMQDSP TVSRVVVDCA NGVGSQPLKT VAGLVKDSLS IELVNTDVRA SELLNNGCGA 

       250        260        270        280        290        300 
DFVKTKQSPP LALEGKIKPN QLYASIDGDA DRLIFYYINQ NRKFHLLDGD KISTALVGYL 

       310        320        330        340        350        360 
NILVKKSGMP FSLGVVQTAY ANGASTEYLQ DLGITTVFTP TGVKHLHKAA KEFDIGVYFE 

       370        380        390        400        410        420 
ANGHGTVLFS DKALANLAHP FFTPSPVQAA AIEQLQSYSV LINQAIGDAI SDLLATISVL 

       430        440        450        460        470        480 
NALHWDASAW SNTYKDLPNK LAKVKVSDRT IYKSTDAERR LVSPDGLQEK IDALVAKYEK 

       490        500        510 
GRSFVRASGT EDVVRVYAEA STKQAADELC EKVCQLVL 

« 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 THR-49 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA90456.1.
PIRS59642.
RefSeqNP_592933.1. NM_001018334.2.

3D structure databases

ProteinModelPortalQ09687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4694067.
STRING4896.SPAC13C5.05c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC13C5.05c.1; SPAC13C5.05c.1:pep; SPAC13C5.05c.
GeneID2542320.
KEGGspo:SPAC13C5.05c.

Organism-specific databases

PomBaseSPAC13C5.05c.

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000210027.
KOK01836.
OMADIVRVYA.
OrthoDBEOG7V1G0D.
PhylomeDBQ09687.

Enzyme and pathway databases

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.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PANTHERPTHR22573:SF3. PTHR22573:SF3. 1 hit.
PfamPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFPIRSF016408. PAGM. 1 hit.
SUPFAMSSF53738. SSF53738. 4 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803381.

Entry information

Entry nameAGM1_SCHPO
AccessionPrimary (citable) accession number: Q09687
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 104 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways