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Protein

Phosphoacetylglucosamine mutase

Gene

PCM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation

Keywords - Ligandi

Magnesium, 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

GO - Cellular componenti

Complete GO annotation...

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.
PRIDEiP38628.

PTM databases

iPTMnetiP38628.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MGS1P401512EBI-2351,EBI-29152

Protein-protein interaction databases

BioGridi36671. 14 interactors.
DIPiDIP-6760N.
IntActiP38628. 1 interactor.
MINTiMINT-637715.

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.
OMAiRVVFYYV.
OrthoDBiEOG092C236M.

Family and domain databases

CDDicd03086. PGM3. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 2 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFiPIRSF016408. PAGM. 1 hit.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP38628.
SMRiP38628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36671. 14 interactors.
DIPiDIP-6760N.
IntActiP38628. 1 interactor.
MINTiMINT-637715.

PTM databases

iPTMnetiP38628.

Proteomic databases

MaxQBiP38628.
PRIDEiP38628.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL058W; YEL058W; YEL058W.
GeneIDi856652.
KEGGisce:YEL058W.

Organism-specific databases

EuPathDBiFungiDB:YEL058W.
SGDiS000000784. PCM1.

Phylogenomic databases

GeneTreeiENSGT00390000000509.
HOGENOMiHOG000210027.
InParanoidiP38628.
KOiK01836.
OMAiRVVFYYV.
OrthoDBiEOG092C236M.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP38628.

Family and domain databases

CDDicd03086. PGM3. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 2 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFiPIRSF016408. PAGM. 1 hit.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGM1_YEAST
AccessioniPrimary (citable) accession number: P38628
Secondary accession number(s): D3DLJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.