ID AGM1_YEAST STANDARD; PRT; 557 AA. AC P38628; DT 01-OCT-1994 (Rel. 30, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Phosphoacetylglucosamine mutase (EC 5.4.2.3) (PAGM) (Acetylglucosamine DE phosphomutase) (N-acetylglucosamine-phosphate mutase). GN Name=PCM1; Synonyms=AGM1; OrderedLocusNames=YEL058W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EBY21-8; RX MEDLINE=94164176; PubMed=8119301; 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 SEQUENCE FROM N.A. RC STRAIN=S288c / AB972; RX MEDLINE=97313264; 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 CHARACTERIZATION. RC STRAIN=EBY21-8; RX MEDLINE=94229071; PubMed=8174553; 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). CC -!- FUNCTION: Interconverts GlcNAc-6-P and GlcNAc-1-P. CC -!- CATALYTIC ACTIVITY: N-acetyl-alpha-D-glucosamine 1-phosphate = N- CC acetyl-D-glucosamine 6-phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: UDP-GlcNAc biosynthesis from Fru-6-P; third step. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. 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; -. DR EMBL; U18795; AAB65029.1; -. DR PIR; S50531; S50531. DR GermOnline; 139062; -. DR SGD; S0000784; PCM1. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IMP. DR InterPro; IPR005841; PG/PMM_mutase. DR InterPro; IPR005844; PG_PMM_ABAI. DR InterPro; IPR005845; PG_PMM_ABAII. DR InterPro; IPR005843; PG_PMM_C. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PROSITE; PS00710; PGM_PMM; 1. KW Isomerase; Phosphorylation; Metal-binding; Magnesium. FT ACT_SITE 67 67 Phosphoserine intermediate (By FT similarity). FT METAL 67 67 Magnesium (via phosphate group) (By FT similarity). FT METAL 298 298 Magnesium (By similarity). FT METAL 300 300 Magnesium (By similarity). FT METAL 302 302 Magnesium (By similarity). FT CONFLICT 15 15 T -> M (in Ref. 1). FT CONFLICT 196 196 Q -> R (in Ref. 1). FT CONFLICT 406 406 E -> G (in Ref. 1). SQ SEQUENCE 557 AA; 62066 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 //