Phosphoacetylglucosamine mutase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38628 (AGM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
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.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome fungal-type cell wall chitin biosynthetic process Inferred from mutant phenotype Ref.4. Source: SGD glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoacetylglucosamine mutase activity Inferred from mutant phenotype Ref.4. Source: SGD phosphoglucomutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MGS1	P40151	2	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

Phosphoserine intermediate

Metal binding

Magnesium; via phosphate group By similarity

Metal binding

298

Magnesium By similarity

Metal binding

300

Magnesium By similarity

Metal binding

302

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.7

Modified residue

Phosphoserine Ref.6 Ref.7

Experimental info

Sequence conflict

T → M in CAA53452. Ref.1

Sequence conflict

196

Q → R in CAA53452. Ref.1

Sequence conflict

406

E → G in CAA53452. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P38628 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 76F17D47D07C920A
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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

« Hide

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] [Europe PMC] [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. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: EBY21-8.
[5]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, MASS SPECTROMETRY. Strain: ADR376.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65 AND SER-67, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75816 Genomic DNA. Translation: CAA53452.1. U18795 Genomic DNA. Translation: AAB65029.1. BK006939 Genomic DNA. Translation: DAA07596.1.
PIR	S50531.
RefSeq	NP_010856.1. NM_001178873.1.
3D structure databases
ProteinModelPortal	P38628.
SMR	P38628. Positions 17-554.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6760N.
IntAct	P38628. 1 interaction.
MINT	MINT-637715.
STRING	4932.YEL058W.
Proteomic databases
PaxDb	P38628.
PeptideAtlas	P38628.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YEL058W; YEL058W; YEL058W.
GeneID	856652.
KEGG	sce:YEL058W.
Organism-specific databases
CYGD	YEL058w.
SGD	S000000784. PCM1.
Phylogenomic databases
eggNOG	COG1109.
GeneTree	ENSGT00390000000509.
HOGENOM	HOG000210027.
KO	K01836.
OMA	DIVRVYA.
OrthoDB	EOG4CVKGN.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13178.
UniPathway	UPA00113; UER00530.
Gene expression databases
Genevestigator	P38628.
GermOnline	YEL058W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.120.10. 2 hits.
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]
PANTHER	PTHR22573:SF3. PTHR22573:SF3. 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.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982631.

Entry information

Entry name

AGM1_YEAST

Accession

Primary (citable) accession number: P38628
Secondary accession number(s): D3DLJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents