ID AGM1_YEAST Reviewed; 557 AA. AC P38628; D3DLJ2; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 11-DEC-2019, entry version 180. DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000305}; DE Short=PAGM; DE EC=5.4.2.3 {ECO:0000269|PubMed:8174553}; DE AltName: Full=Acetylglucosamine phosphomutase; DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000303|PubMed:8174553}; DE AltName: Full=PGM-complementing protein 1 {ECO:0000303|PubMed:8119301}; GN Name=PCM1 {ECO:0000303|PubMed:8119301}; GN Synonyms=AGM1 {ECO:0000303|PubMed:8174553}; GN OrderedLocusNames=YEL058W {ECO:0000312|SGD:S000000784}; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=EBY21-8; RX PubMed=8119301; DOI=10.1111/j.1432-1033.1994.tb18601.x; RA Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.; RT "A family of hexosephosphate mutases in Saccharomyces cerevisiae."; RL Eur. J. Biochem. 220:83-96(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE. RC STRAIN=EBY21-8; RX PubMed=8174553; DOI=10.1111/j.1432-1033.1994.tb18787.x; RA Hofmann M., Boles E., Zimmermann F.K.; RT "Characterization of the essential yeast gene encoding N-acetylglucosamine- RT phosphate mutase."; RL Eur. J. Biochem. 221:741-747(1994). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). 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 (PubMed:8174553). Also has CC phosphoglucomutase activity (PubMed:8119301). CC {ECO:0000269|PubMed:8119301, ECO:0000269|PubMed:8174553}. 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; Evidence={ECO:0000269|PubMed:8174553}; 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:0000305|PubMed:8174553}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- DISRUPTION PHENOTYPE: Results in undivided strings of cells and growth CC arrest after approximately 5 division cycles. CC {ECO:0000269|PubMed:8174553}. CC -!- MISCELLANEOUS: Present with 14700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X75816; CAA53452.1; -; Genomic_DNA. DR EMBL; U18795; AAB65029.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07596.1; -; Genomic_DNA. DR PIR; S50531; S50531. DR RefSeq; NP_010856.1; NM_001178873.1. DR SMR; P38628; -. DR BioGrid; 36671; 17. DR DIP; DIP-6760N; -. DR IntAct; P38628; 1. DR STRING; 4932.YEL058W; -. DR iPTMnet; P38628; -. DR MaxQB; P38628; -. DR PaxDb; P38628; -. DR PRIDE; P38628; -. DR EnsemblFungi; YEL058W_mRNA; YEL058W; YEL058W. DR GeneID; 856652; -. DR KEGG; sce:YEL058W; -. DR EuPathDB; FungiDB:YEL058W; -. DR SGD; S000000784; PCM1. DR HOGENOM; HOG000210027; -. DR InParanoid; P38628; -. DR KO; K01836; -. DR OMA; PGDRCCS; -. DR BioCyc; MetaCyc:YEL058W-MONOMER; -. DR BioCyc; YEAST:YEL058W-MONOMER; -. DR Reactome; R-SCE-446210; Synthesis of UDP-N-acetyl-glucosamine. DR UniPathway; UPA00113; UER00530. DR PRO; PR:P38628; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P38628; protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IMP:SGD. 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; IMP:SGD. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central. 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; IPR016066; A-D-PHexomutase_CS. 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. DR PROSITE; PS00710; PGM_PMM; 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..557 FT /note="Phosphoacetylglucosamine mutase" FT /id="PRO_0000148019" FT REGION 395..397 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT REGION 522..526 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT ACT_SITE 67 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT METAL 67 FT /note="Magnesium; via phosphate group" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT METAL 298 FT /note="Magnesium" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT METAL 300 FT /note="Magnesium" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT METAL 302 FT /note="Magnesium" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT BINDING 531 FT /note="Substrate" FT /evidence="ECO:0000250|UniProtKB:Q9P4V2" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17330950" FT CONFLICT 15 FT /note="T -> M (in Ref. 1; CAA53452)" FT /evidence="ECO:0000305" FT CONFLICT 196 FT /note="Q -> R (in Ref. 1; CAA53452)" FT /evidence="ECO:0000305" FT CONFLICT 406 FT /note="E -> G (in Ref. 1; CAA53452)" FT /evidence="ECO:0000305" SQ SEQUENCE 557 AA; 62067 MW; 76F17D47D07C920A CRC64; MKVDYEQLCK LYDDTCRTKN VQFSYGTAGF RTLAKNLDTV MFSTGILAVL RSLKLQGQYV GVMITASHNP YQDNGVKIVE PDGSMLLATW EPYAMQLANA ASFATNFEEF RVELAKLIEH EKIDLNTTVV PHIVVGRDSR ESSPYLLRCL TSSMASVFHA QVLDLGCVTT PQLHYITDLS NRRKLEGDTA PVATEQDYYS FFIGAFNELF ATYQLEKRLS VPKLFIDTAN GIGGPQLKKL LASEDWDVPA EQVEVINDRS DVPELLNFEC GADYVKTNQR LPKGLSPSSF DSLYCSFDGD ADRVVFYYVD SGSKFHLLDG DKISTLFAKF LSKQLELAHL EHSLKIGVVQ TAYANGSSTA YIKNTLHCPV SCTKTGVKHL HHEAATQYDI GIYFEANGHG TIIFSEKFHR TIKSELSKSK LNGDTLALRT LKCFSELINQ TVGDAISDML AVLATLAILK MSPMDWDEEY TDLPNKLVKC IVPDRSIFQT TDQERKLLNP VGLQDKIDLV VAKYPMGRSF VRASGTEDAV RVYAECKDSS KLGQFCDEVV EHVKASA //