ID PCM1_YEAST STANDARD; PRT; 557 AA. AC P38628; DT 01-OCT-1994 (Rel. 30, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE PHOSPHOACETYLGLUCOSAMINE MUTASE (EC 5.4.2.3) (ACETYLGLUCOSAMINE DE PHOSPHOMUTASE) (N-ACETYLGLUCOSAMINE-PHOSPHATE MUTASE). GN PCM1 OR AGM1 OR YEL058W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EBY21-8; RX MEDLINE; 94164176. 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; RA Dietrich F.S., Mulligan J.T., Hennessey K.M., Allen E., Araujo R., RA Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., RA Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R., Kayser A., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., RA Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., RA Taylor P., Wei Y., Yelton M., Botstein D., Davis R.W.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP CHARACTERIZATION. RC STRAIN=EBY21-8; RX MEDLINE; 94229071. 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 -!- CATALYTIC ACTIVITY: N-ACETYL-D-GLUCOSAMINE 1-PHOSPHATE = N-ACETYL- CC D-GLUCOSAMINE 6-PHOSPHATE. CC -!- SIMILARITY: TO PHOSPHOGLUCOMUTASES AND PHOSPHOMANNOMUTASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; S40263; S40263. DR SGD; L0001351; PCM1. DR INTERPRO; IPR001485; -. DR PFAM; PF00408; PGM_PMM; 1. DR PROSITE; PS00710; PGM_PMM; 1. KW Isomerase. FT ACT_SITE 67 67 FORMS THE PHOSPHOSERINE INTERMEDIATE FT (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 //