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Protein

Phosphoacetylglucosamine mutase 2

Gene

SPAC1296.01c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathway:iUDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I).By similarity
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glucosamine 6-phosphate N-acetyltransferase (gna1)
  2. Phosphoacetylglucosamine mutase 2 (SPAC1296.01c), Phosphoacetylglucosamine mutase 1 (SPAC13C5.05c)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei77 – 771Phosphoserine intermediateBy similarity
Metal bindingi77 – 771Magnesium; via phosphate groupBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity
Metal bindingi294 – 2941MagnesiumBy similarity
Metal bindingi296 – 2961MagnesiumBy similarity
Binding sitei519 – 5191SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_306868. Synthesis of UDP-N-acetyl-glucosamine.
UniPathwayiUPA00113; UER00530.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoacetylglucosamine mutase 2By similarity (EC:5.4.2.3By similarity)
Short name:
PAGM
Alternative name(s):
Acetylglucosamine phosphomutaseBy similarity
N-acetylglucosamine-phosphate mutaseBy similarity
Gene namesi
ORF Names:SPAC1296.01cImported, SPAC22F3.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1296.01c.
PomBaseiSPAC1296.01c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • mannosyltransferase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Phosphoacetylglucosamine mutase 2PRO_0000148018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei82 – 821Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09770.

Interactioni

Protein-protein interaction databases

BioGridi280512. 27 interactions.
MINTiMINT-4694906.

Structurei

3D structure databases

ProteinModelPortaliQ09770.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni385 – 3873Substrate bindingBy similarity
Regioni510 – 5145Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000210027.
InParanoidiQ09770.
KOiK01836.
OMAiHNASSEN.
OrthoDBiEOG7V1G0D.
PhylomeDBiQ09770.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 1 hit.
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.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
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.

Sequencei

Sequence statusi: Complete.

Q09770-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAEDSDSI VNEFVTAIVR ESDKFAKVHS YPMQYGTGGY RADAELLSSV
60 70 80 90 100
AFRTGVIASF LSAKLHGQPV GLMVTASHNA SSENGLKIVN ILSSLDSSKW
110 120 130 140 150
EAYLDQVVNA DSADELTVCL TSILKKAKII PGSEARVFVG YDSRSTSEIL
160 170 180 190 200
AQAVIDGIVV CKAKYENFGL LTTPQLHYMV KASQTYGTPD AIGEPTERGY
210 220 230 240 250
FEKLSKAYQS LMTGKKIKGT VLIDAANGVG AAKIKELAKY IDPKLFPIEI
260 270 280 290 300
VNDNIDNPEL LNNSCGADFV RTQQKPPNGI SAPKHARCAS FDGDADRIVY
310 320 330 340 350
FAFGSHSFHL LDGDKICALF AQFLIDLIRS TGLDLQVGIV QTAYANGAST
360 370 380 390 400
AFFQKTLKVP VLCVSPGLKH LYHAAQAYDV GVFFEANGHG TILVSHAALS
410 420 430 440 450
KIISHEVLSP AQFNALKTLK TVFELINQTD GDAITNLLLV EVILAHKNCT
460 470 480 490 500
LKEWNQLYSE IPSRLIRCEV EDRSIYTTTD AEQKLVTPEG LQEKIDALVA
510 520 530 540
KYTGGRAFVR SSGTEDAVRV YAEASSRGES EDLALRIVEL LH
Length:542
Mass (Da):58,916
Last modified:August 29, 2001 - v2
Checksum:i131871396737609E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91066.1.
PIRiT37562.
T38190. S62416.
RefSeqiNP_593040.2. NM_001018439.3.

Genome annotation databases

EnsemblFungiiSPAC1296.01c.1; SPAC1296.01c.1:pep; SPAC1296.01c.
GeneIDi3361436.
KEGGispo:SPAC1296.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91066.1.
PIRiT37562.
T38190. S62416.
RefSeqiNP_593040.2. NM_001018439.3.

3D structure databases

ProteinModelPortaliQ09770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280512. 27 interactions.
MINTiMINT-4694906.

Proteomic databases

MaxQBiQ09770.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1296.01c.1; SPAC1296.01c.1:pep; SPAC1296.01c.
GeneIDi3361436.
KEGGispo:SPAC1296.01c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1296.01c.
PomBaseiSPAC1296.01c.

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000210027.
InParanoidiQ09770.
KOiK01836.
OMAiHNASSEN.
OrthoDBiEOG7V1G0D.
PhylomeDBiQ09770.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00530.
ReactomeiREACT_306868. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

NextBioi20811483.
PROiQ09770.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 1 hit.
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.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
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.
ProtoNetiSearch...

Publicationsi

  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.
    , 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. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiAGM2_SCHPO
AccessioniPrimary (citable) accession number: Q09770
Secondary accession number(s): O94610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 29, 2001
Last modified: July 22, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.