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   27-MAR-2024, entry version 154.
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; 30.
DR   STRING; 284812.Q09770; -.
DR   iPTMnet; Q09770; -.
DR   MaxQB; Q09770; -.
DR   PaxDb; 4896-SPAC1296-01c-1; -.
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; VLDDGCC; -.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd03086; PGM3; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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; IPR049023; AMG1_II.
DR   InterPro; IPR049022; AMG1_III.
DR   InterPro; IPR016657; PAGM.
DR   PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   PANTHER; PTHR45955:SF3; PHOSPHOACETYLGLUCOSAMINE MUTASE 2; 1.
DR   Pfam; PF21405; AMG1_II; 1.
DR   Pfam; PF21404; AMG1_III; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PIRSF; PIRSF016408; PAGM; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
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
//