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P38628 (AGM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MGS1P401512EBI-2351,EBI-29152

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Phosphoacetylglucosamine mutase
PRO_0000148019

Sites

Active site671Phosphoserine intermediate
Metal binding671Magnesium; via phosphate group By similarity
Metal binding2981Magnesium By similarity
Metal binding3001Magnesium By similarity
Metal binding3021Magnesium By similarity

Amino acid modifications

Modified residue671Phosphoserine Ref.6

Experimental info

Sequence conflict151T → M in CAA53452. Ref.1
Sequence conflict1961Q → R in CAA53452. Ref.1
Sequence conflict4061E → G in CAA53452. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38628 [UniParc].

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

FASTA55762,067
        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' 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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS50531.
RefSeqNP_010856.1. NM_001178873.1.

3D structure databases

ProteinModelPortalP38628.
SMRP38628. Positions 17-554.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36671. 14 interactions.
DIPDIP-6760N.
IntActP38628. 1 interaction.
MINTMINT-637715.
STRING4932.YEL058W.

Proteomic databases

PaxDbP38628.
PeptideAtlasP38628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL058W; YEL058W; YEL058W.
GeneID856652.
KEGGsce:YEL058W.

Organism-specific databases

CYGDYEL058w.
SGDS000000784. PCM1.

Phylogenomic databases

eggNOGCOG1109.
GeneTreeENSGT00390000000509.
HOGENOMHOG000210027.
KOK01836.
OMADIVRVYA.
OrthoDBEOG7V1G0D.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13178.
YEAST:YEL058W-MONOMER.
UniPathwayUPA00113; UER00530.

Gene expression databases

GenevestigatorP38628.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 2 hits.
InterProIPR005844. 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]
PANTHERPTHR22573:SF3. PTHR22573:SF3. 1 hit.
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFPIRSF016408. PAGM. 1 hit.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982631.
PROP38628.

Entry information

Entry nameAGM1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways