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 28-MAR-2018, entry version 169. 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; OC Saccharomycetes; 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., RA Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., RA Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., RA Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., RA Smith V., Taylor P., Wei Y., 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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- RT acetylglucosamine-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., RA Dephoure N., 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 RP BY 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 RT phosphoproteome 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 RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P CC during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a CC biosynthetic precursor of chitin and also supplies the amino CC sugars for N-linked oligosaccharides of glycoproteins CC (PubMed:8174553). Also has phosphoglucomutase activity CC (PubMed:8119301). {ECO:0000269|PubMed:8119301, CC ECO:0000269|PubMed:8174553}. CC -!- CATALYTIC ACTIVITY: N-acetyl-alpha-D-glucosamine 1-phosphate = N- CC acetyl-D-glucosamine 6-phosphate. {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. CC {ECO:0000250|UniProtKB:Q9P4V2}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate CC from alpha-D-glucosamine 6-phosphate (route I): step 2/2. CC {ECO:0000305|PubMed:8174553}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC Nucleus {ECO:0000269|PubMed:14562095}. CC -!- DISRUPTION PHENOTYPE: Results in undivided strings of cells and CC growth 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. CC {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 ProteinModelPortal; P38628; -. DR SMR; P38628; -. DR BioGrid; 36671; 14. DR DIP; DIP-6760N; -. DR IntAct; P38628; 5. DR STRING; 4932.YEL058W; -. DR iPTMnet; P38628; -. DR MaxQB; P38628; -. DR PaxDb; P38628; -. DR PRIDE; P38628; -. DR EnsemblFungi; YEL058W; YEL058W; YEL058W. DR GeneID; 856652; -. DR KEGG; sce:YEL058W; -. DR EuPathDB; FungiDB:YEL058W; -. DR SGD; S000000784; PCM1. DR GeneTree; ENSGT00390000000509; -. DR HOGENOM; HOG000210027; -. DR InParanoid; P38628; -. DR KO; K01836; -. DR OMA; LHYMVCC; -. DR OrthoDB; EOG092C236M; -. 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 GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IMP:SGD. 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; KW Complete proteome; Cytoplasm; Isomerase; Magnesium; Metal-binding; KW Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1 557 Phosphoacetylglucosamine mutase. FT /FTId=PRO_0000148019. FT REGION 395 397 Substrate binding. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT REGION 522 526 Substrate binding. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT ACT_SITE 67 67 Phosphoserine intermediate. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT METAL 67 67 Magnesium; via phosphate group. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT METAL 298 298 Magnesium. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT METAL 300 300 Magnesium. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT METAL 302 302 Magnesium. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT BINDING 531 531 Substrate. FT {ECO:0000250|UniProtKB:Q9P4V2}. FT MOD_RES 67 67 Phosphoserine. FT {ECO:0000244|PubMed:17330950}. FT CONFLICT 15 15 T -> M (in Ref. 1; CAA53452). FT {ECO:0000305}. FT CONFLICT 196 196 Q -> R (in Ref. 1; CAA53452). FT {ECO:0000305}. FT CONFLICT 406 406 E -> G (in Ref. 1; CAA53452). FT {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 //