Reviewed, UniProtKB/Swiss-Prot P38628 (AGM1_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphoacetylglucosamine mutase
      Short name=PAGM
    EC=5.4.2.3
Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase

Gene names

Name:	PCM1
Synonyms:	AGM1
Ordered Locus Names:	YEL058W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Interconverts GlcNAc-6-P and GlcNAc-1-P.
Catalytic activity	N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
Post-translational modification	Phosphorylation at Ser-67 is involved in the reaction mechanism.
Miscellaneous	Present with 14700 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall chitin biosynthetic process Ref.3 Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoacetylglucosamine mutase activity Ref.3 Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MGS1	P40151	1	EBI-2351,EBI-29152

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 557	557	Phosphoacetylglucosamine mutase		PRO_0000148019
Sites
	Active site	67	1	Phosphoserine intermediate
	Metal binding	67	1	Magnesium; via phosphate group By similarity
	Metal binding	298	1	Magnesium By similarity
	Metal binding	300	1	Magnesium By similarity
	Metal binding	302	1	Magnesium By similarity
Amino acid modifications
	Modified residue	65	1	Phosphothreonine Ref.6
	Modified residue	67	1	Phosphoserine Ref.6 Ref.5
Experimental info
	Sequence conflict	15	1	T → M in CAA53452. Ref.1
	Sequence conflict	196	1	Q → R in CAA53452. Ref.1
	Sequence conflict	406	1	E → G in CAA53452. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38628-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 76F17D47D07C920A	FASTA	557	62,067
	10 20 30 40 50 60 MKVDYEQLCK LYDDTCRTKN VQFSYGTAGF RTLAKNLDTV MFSTGILAVL RSLKLQGQYV 70 80 90 100 110 120 GVMITASHNP YQDNGVKIVE PDGSMLLATW EPYAMQLANA ASFATNFEEF RVELAKLIEH 130 140 150 160 170 180 EKIDLNTTVV PHIVVGRDSR ESSPYLLRCL TSSMASVFHA QVLDLGCVTT PQLHYITDLS 190 200 210 220 230 240 NRRKLEGDTA PVATEQDYYS FFIGAFNELF ATYQLEKRLS VPKLFIDTAN GIGGPQLKKL 250 260 270 280 290 300 LASEDWDVPA EQVEVINDRS DVPELLNFEC GADYVKTNQR LPKGLSPSSF DSLYCSFDGD 310 320 330 340 350 360 ADRVVFYYVD SGSKFHLLDG DKISTLFAKF LSKQLELAHL EHSLKIGVVQ TAYANGSSTA 370 380 390 400 410 420 YIKNTLHCPV SCTKTGVKHL HHEAATQYDI GIYFEANGHG TIIFSEKFHR TIKSELSKSK 430 440 450 460 470 480 LNGDTLALRT LKCFSELINQ TVGDAISDML AVLATLAILK MSPMDWDEEY TDLPNKLVKC 490 500 510 520 530 540 IVPDRSIFQT TDQERKLLNP VGLQDKIDLV VAKYPMGRSF VRASGTEDAV RVYAECKDSS 550 KLGQFCDEVV EHVKASA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of hexosephosphate mutases in Saccharomyces cerevisiae." Boles E., Liebetrau W., Hofmann M., Zimmermann F.K. Eur. J. Biochem. 220:83-96(1994) [PubMed: 8119301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EBY21-8.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase." Hofmann M., Boles E., Zimmermann F.K. Eur. J. Biochem. 221:741-747(1994) [PubMed: 8174553] [Abstract] Cited for: CHARACTERIZATION. Strain: EBY21-8.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, MASS SPECTROMETRY.
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65 AND SER-67, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X75816 Genomic DNA. Translation: CAA53452.1. U18795 Genomic DNA. Translation: AAB65029.1.
PIR	S50531.
RefSeq	NP_010856.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6760N.
IntAct	P38628. 6 interactions.
STRING	P38628.
Proteomic databases
PeptideAtlas	P38628.
Genome annotation databases
Ensembl	YEL058W; YEL058W; YEL058W; Saccharomyces cerevisiae. [Genome view]
GeneID	856652.
GenomeReviews	Gene locus YEL058W in contig U00092_GR.
KEGG	sce:YEL058W.
NMPDR	fig|4932.3.peg.1905.
Organism-specific databases
CYGD	YEL058w.
SGD	S000000784. PCM1.
Phylogenomic databases
HOGENOM	P38628.
OMA	NLHPIAH.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13178.
BRENDA	5.4.2.3. 250.
Gene expression databases
ArrayExpress	P38628.
Genevestigator	P38628.
GermOnline	YEL058W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR016657. PAGM. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 1 hit.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PIRSF	PIRSF016408. PAGM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982631.

Entry information

Entry name

AGM1_YEAST

Accession

Primary (citable) accession number: P38628

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)