AGM2_SCHPO
ID AGM2_SCHPO Reviewed; 542 AA.
AC Q09770; O94610;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphoacetylglucosamine mutase 2 {ECO:0000250|UniProtKB:P38628};
DE Short=PAGM;
DE EC=5.4.2.3 {ECO:0000250|UniProtKB:P38628};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000250|UniProtKB:P38628};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000250|UniProtKB:P38628};
GN ORFNames=SPAC1296.01c {ECO:0000312|PomBase:SPAC1296.01c}, SPAC22F3.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-82, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC the synthesis of uridine diphosphate/UDP-GlcNAc, which is a
CC biosynthetic precursor of chitin and also supplies the amino sugars for
CC N-linked oligosaccharides of glycoproteins.
CC {ECO:0000250|UniProtKB:P38628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513,
CC ChEBI:CHEBI:57776; EC=5.4.2.3;
CC Evidence={ECO:0000250|UniProtKB:P38628};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9P4V2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC {ECO:0000250|UniProtKB:P38628}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91066.1; -; Genomic_DNA.
DR PIR; T37562; T37562.
DR PIR; T38190; S62416.
DR RefSeq; NP_593040.2; NM_001018439.3.
DR AlphaFoldDB; Q09770; -.
DR SMR; Q09770; -.
DR BioGRID; 280512; 29.
DR STRING; 4896.SPAC1296.01c.1; -.
DR iPTMnet; Q09770; -.
DR MaxQB; Q09770; -.
DR PaxDb; Q09770; -.
DR PRIDE; Q09770; -.
DR EnsemblFungi; SPAC1296.01c.1; SPAC1296.01c.1:pep; SPAC1296.01c.
DR PomBase; SPAC1296.01c; -.
DR VEuPathDB; FungiDB:SPAC1296.01c; -.
DR eggNOG; KOG2537; Eukaryota.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; Q09770; -.
DR OMA; NAFRTED; -.
DR PhylomeDB; Q09770; -.
DR UniPathway; UPA00113; UER00530.
DR PRO; PR:Q09770; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; ISO:PomBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; ISO:PomBase.
DR CDD; cd03086; PGM3; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016657; PAGM.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PIRSF; PIRSF016408; PAGM; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Cytoplasm;
KW Isomerase; Magnesium; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..542
FT /note="Phosphoacetylglucosamine mutase 2"
FT /id="PRO_0000148018"
FT ACT_SITE 77
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 385..387
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 510..514
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 519
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 542 AA; 58916 MW; 131871396737609E CRC64;
MSDAEDSDSI VNEFVTAIVR ESDKFAKVHS YPMQYGTGGY RADAELLSSV AFRTGVIASF
LSAKLHGQPV GLMVTASHNA SSENGLKIVN ILSSLDSSKW EAYLDQVVNA DSADELTVCL
TSILKKAKII PGSEARVFVG YDSRSTSEIL AQAVIDGIVV CKAKYENFGL LTTPQLHYMV
KASQTYGTPD AIGEPTERGY FEKLSKAYQS LMTGKKIKGT VLIDAANGVG AAKIKELAKY
IDPKLFPIEI VNDNIDNPEL LNNSCGADFV RTQQKPPNGI SAPKHARCAS FDGDADRIVY
FAFGSHSFHL LDGDKICALF AQFLIDLIRS TGLDLQVGIV QTAYANGAST AFFQKTLKVP
VLCVSPGLKH LYHAAQAYDV GVFFEANGHG TILVSHAALS KIISHEVLSP AQFNALKTLK
TVFELINQTD GDAITNLLLV EVILAHKNCT LKEWNQLYSE IPSRLIRCEV EDRSIYTTTD
AEQKLVTPEG LQEKIDALVA KYTGGRAFVR SSGTEDAVRV YAEASSRGES EDLALRIVEL
LH
