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Protein

Phosphoacetylglucosamine mutase

Gene

PCM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins (PubMed:8174553). Also has phosphoglucomutase activity (PubMed:8119301).2 Publications

Miscellaneous

Present with 14700 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I).1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glucosamine 6-phosphate N-acetyltransferase (GNA1)
  2. Phosphoacetylglucosamine mutase (PCM1)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei67Phosphoserine intermediateBy similarity1
Metal bindingi67Magnesium; via phosphate groupBy similarity1
Metal bindingi298MagnesiumBy similarity1
Metal bindingi300MagnesiumBy similarity1
Metal bindingi302MagnesiumBy similarity1
Binding sitei531SubstrateBy similarity1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphoacetylglucosamine mutase activity Source: SGD

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • fungal-type cell wall chitin biosynthetic process Source: SGD
  • UDP-N-acetylglucosamine biosynthetic process Source: GO_Central

Keywordsi

Molecular functionIsomerase
Biological processCarbohydrate metabolism, Cell wall biogenesis/degradation
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YEL058W-MONOMER
YEAST:YEL058W-MONOMER
ReactomeiR-SCE-446210 Synthesis of UDP-N-acetyl-glucosamine
UniPathwayiUPA00113; UER00530

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoacetylglucosamine mutaseCurated (EC:5.4.2.31 Publication)
Short name:
PAGM
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase1 Publication
PGM-complementing protein 11 Publication
Gene namesi
Name:PCM11 Publication
Synonyms:AGM11 Publication
Ordered Locus Names:YEL058WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL058W
SGDiS000000784 PCM1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Results in undivided strings of cells and growth arrest after approximately 5 division cycles.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480191 – 557Phosphoacetylglucosamine mutaseAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38628
PaxDbiP38628
PRIDEiP38628

PTM databases

iPTMnetiP38628

Interactioni

Protein-protein interaction databases

BioGridi36671, 14 interactors
DIPiDIP-6760N
IntActiP38628, 1 interactor
STRINGi4932.YEL058W

Structurei

3D structure databases

ProteinModelPortaliP38628
SMRiP38628
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni395 – 397Substrate bindingBy similarity3
Regioni522 – 526Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000000509
HOGENOMiHOG000210027
InParanoidiP38628
KOiK01836
OMAiLHYMVCC
OrthoDBiEOG092C236M

Family and domain databases

CDDicd03086 PGM3, 1 hit
InterProiView protein in InterPro
IPR005844 A-D-PHexomutase_a/b/a-I
IPR016055 A-D-PHexomutase_a/b/a-I/II/III
IPR005843 A-D-PHexomutase_C
IPR036900 A-D-PHexomutase_C_sf
IPR016066 A-D-PHexomutase_CS
IPR016657 PAGM
PfamiView protein in Pfam
PF02878 PGM_PMM_I, 1 hit
PF00408 PGM_PMM_IV, 1 hit
PIRSFiPIRSF016408 PAGM, 1 hit
SUPFAMiSSF53738 SSF53738, 3 hits
SSF55957 SSF55957, 1 hit
PROSITEiView protein in PROSITE
PS00710 PGM_PMM, 1 hit

Sequencei

Sequence statusi: Complete.

P38628-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVDYEQLCK LYDDTCRTKN VQFSYGTAGF RTLAKNLDTV MFSTGILAVL
60 70 80 90 100
RSLKLQGQYV GVMITASHNP YQDNGVKIVE PDGSMLLATW EPYAMQLANA
110 120 130 140 150
ASFATNFEEF RVELAKLIEH EKIDLNTTVV PHIVVGRDSR ESSPYLLRCL
160 170 180 190 200
TSSMASVFHA QVLDLGCVTT PQLHYITDLS NRRKLEGDTA PVATEQDYYS
210 220 230 240 250
FFIGAFNELF ATYQLEKRLS VPKLFIDTAN GIGGPQLKKL LASEDWDVPA
260 270 280 290 300
EQVEVINDRS DVPELLNFEC GADYVKTNQR LPKGLSPSSF DSLYCSFDGD
310 320 330 340 350
ADRVVFYYVD SGSKFHLLDG DKISTLFAKF LSKQLELAHL EHSLKIGVVQ
360 370 380 390 400
TAYANGSSTA YIKNTLHCPV SCTKTGVKHL HHEAATQYDI GIYFEANGHG
410 420 430 440 450
TIIFSEKFHR TIKSELSKSK LNGDTLALRT LKCFSELINQ TVGDAISDML
460 470 480 490 500
AVLATLAILK MSPMDWDEEY TDLPNKLVKC IVPDRSIFQT TDQERKLLNP
510 520 530 540 550
VGLQDKIDLV VAKYPMGRSF VRASGTEDAV RVYAECKDSS KLGQFCDEVV

EHVKASA
Length:557
Mass (Da):62,067
Last modified:February 1, 1995 - v2
Checksum:i76F17D47D07C920A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15T → M in CAA53452 (PubMed:8119301).Curated1
Sequence conflicti196Q → R in CAA53452 (PubMed:8119301).Curated1
Sequence conflicti406E → G in CAA53452 (PubMed:8119301).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75816 Genomic DNA Translation: CAA53452.1
U18795 Genomic DNA Translation: AAB65029.1
BK006939 Genomic DNA Translation: DAA07596.1
PIRiS50531
RefSeqiNP_010856.1, NM_001178873.1

Genome annotation databases

EnsemblFungiiYEL058W; YEL058W; YEL058W
GeneIDi856652
KEGGisce:YEL058W

Similar proteinsi

Entry informationi

Entry nameiAGM1_YEAST
AccessioniPrimary (citable) accession number: P38628
Secondary accession number(s): D3DLJ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 170 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health