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Protein

Phosphoacetylglucosamine mutase

Gene

Pgm3

Organism
Mus musculus (Mouse)
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, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.By similarity

Catalytic activityi

N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.By similarity

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).By similarity
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glucosamine 6-phosphate N-acetyltransferase (Gnpnat1)
  2. Phosphoacetylglucosamine mutase (Pgm3)
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 sitei64Phosphoserine intermediateBy similarity1
Metal bindingi64Magnesium; via phosphate groupBy similarity1
Metal bindingi276MagnesiumBy similarity1
Metal bindingi278MagnesiumBy similarity1
Metal bindingi280MagnesiumBy similarity1
Binding sitei505SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB-KW
  • glucose 1-phosphate metabolic process Source: MGI
  • hemopoiesis Source: MGI
  • protein N-linked glycosylation Source: UniProtKB
  • protein O-linked glycosylation Source: UniProtKB
  • spermatogenesis Source: MGI
  • UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-446210. Synthesis of UDP-N-acetyl-glucosamine.
UniPathwayiUPA00113; UER00530.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoacetylglucosamine mutaseCurated (EC:5.4.2.3By similarity)
Short name:
PAGM
Alternative name(s):
Acetylglucosamine phosphomutaseCurated
N-acetylglucosamine-phosphate mutaseCurated
Phosphoglucomutase-3Imported
Short name:
PGM 3
Gene namesi
Name:Pgm3Imported
Synonyms:Agm1, Pgm-3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97566. Pgm3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480141 – 542Phosphoacetylglucosamine mutaseAdd BLAST542

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei62PhosphothreonineCombined sources1
Modified residuei64PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CYR6.
MaxQBiQ9CYR6.
PaxDbiQ9CYR6.
PRIDEiQ9CYR6.

PTM databases

iPTMnetiQ9CYR6.
PhosphoSitePlusiQ9CYR6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000056131.
CleanExiMM_PGM3.
ExpressionAtlasiQ9CYR6. baseline and differential.
GenevisibleiQ9CYR6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070871.

Structurei

Secondary structure

1542
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi449 – 454Combined sources6
Beta strandi459 – 462Combined sources4
Beta strandi470 – 474Combined sources5
Helixi477 – 487Combined sources11
Beta strandi488 – 496Combined sources9
Beta strandi498 – 512Combined sources15
Helixi513 – 530Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WJWNMR-A442-540[»]
ProteinModelPortaliQ9CYR6.
SMRiQ9CYR6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CYR6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 372Substrate bindingBy similarity3
Regioni496 – 500Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiKOG2537. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000000509.
HOVERGENiHBG024321.
InParanoidiQ9CYR6.
KOiK01836.
OMAiEPFTRCV.
OrthoDBiEOG091G065D.
PhylomeDBiQ9CYR6.
TreeFamiTF105670.

Family and domain databases

CDDicd03086. PGM3. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 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. 2 hits.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFiPIRSF016408. PAGM. 1 hit.
SUPFAMiSSF53738. SSF53738. 4 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CYR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLEAVCKRS ALHAKPQGLI LQYGTAGFRT NAQHLDHIMF RMGLLAVLRS
60 70 80 90 100
KQTRSTIGVM VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLASAEEQ
110 120 130 140 150
DVRQVLAAIV EKEAVDLTQT AFVVIARDTR PSSEKLSQSV IDGVTVLGGQ
160 170 180 190 200
FHDYGLLTTP QLHYMVYCRN SGGRYGQATV EGYCQKLSKA FVDLTNQVSC
210 220 230 240 250
SGDVKRSVKV DCANGIGALK LREMEHYFSR GLSVLLFNDG TQGRLNHLCG
260 270 280 290 300
ADFVKSQQKP PQGIEMKSGE RCCSFDGDAD RIVYYYCDAD GHFHLIDGDK
310 320 330 340 350
IATLISSFLK ELLLEIGESV NLGVVQTAYA NGSSTRYLEE VMKVPVYCTK
360 370 380 390 400
TGVKHLHHKA QEFDIGVYFE ANGHGTALFS EAVEVKIKRL AQELDDGKGK
410 420 430 440 450
AARTLASIID LFNQAAGDAI SDMLVIEAIL ALKGLTVQQW DAIYVDLPNR
460 470 480 490 500
QLKVKVADRR VISTTDAERQ AVTPPGLQEA INDLVKKYTL ARAFVRPSGT
510 520 530 540
EDIVRVYAEA NSQESADRLA YEVSLLVFQL AGGIGERPQP TF
Length:542
Mass (Da):59,453
Last modified:June 1, 2001 - v1
Checksum:iB00E3D0F38BE4090
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013402 mRNA. Translation: BAB28834.1.
AK028066 mRNA. Translation: BAC25733.1.
AK049337 mRNA. Translation: BAC33692.1.
AK051706 mRNA. Translation: BAC34728.1.
AK160913 mRNA. Translation: BAE36087.1.
AK165513 mRNA. Translation: BAE38229.1.
AK169082 mRNA. Translation: BAE40866.1.
AK169787 mRNA. Translation: BAE41366.1.
BC138700 mRNA. Translation: AAI38701.1.
CCDSiCCDS23381.1.
RefSeqiNP_001157218.1. NM_001163746.1.
NP_082628.3. NM_028352.4.
UniGeneiMm.390201.

Genome annotation databases

EnsembliENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.
GeneIDi109785.
KEGGimmu:109785.
UCSCiuc009qxm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013402 mRNA. Translation: BAB28834.1.
AK028066 mRNA. Translation: BAC25733.1.
AK049337 mRNA. Translation: BAC33692.1.
AK051706 mRNA. Translation: BAC34728.1.
AK160913 mRNA. Translation: BAE36087.1.
AK165513 mRNA. Translation: BAE38229.1.
AK169082 mRNA. Translation: BAE40866.1.
AK169787 mRNA. Translation: BAE41366.1.
BC138700 mRNA. Translation: AAI38701.1.
CCDSiCCDS23381.1.
RefSeqiNP_001157218.1. NM_001163746.1.
NP_082628.3. NM_028352.4.
UniGeneiMm.390201.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WJWNMR-A442-540[»]
ProteinModelPortaliQ9CYR6.
SMRiQ9CYR6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070871.

PTM databases

iPTMnetiQ9CYR6.
PhosphoSitePlusiQ9CYR6.

Proteomic databases

EPDiQ9CYR6.
MaxQBiQ9CYR6.
PaxDbiQ9CYR6.
PRIDEiQ9CYR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.
GeneIDi109785.
KEGGimmu:109785.
UCSCiuc009qxm.2. mouse.

Organism-specific databases

CTDi5238.
MGIiMGI:97566. Pgm3.

Phylogenomic databases

eggNOGiKOG2537. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000000509.
HOVERGENiHBG024321.
InParanoidiQ9CYR6.
KOiK01836.
OMAiEPFTRCV.
OrthoDBiEOG091G065D.
PhylomeDBiQ9CYR6.
TreeFamiTF105670.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00530.
ReactomeiR-MMU-446210. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

EvolutionaryTraceiQ9CYR6.
PROiQ9CYR6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000056131.
CleanExiMM_PGM3.
ExpressionAtlasiQ9CYR6. baseline and differential.
GenevisibleiQ9CYR6. MM.

Family and domain databases

CDDicd03086. PGM3. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 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. 2 hits.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFiPIRSF016408. PAGM. 1 hit.
SUPFAMiSSF53738. SSF53738. 4 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGM1_MOUSE
AccessioniPrimary (citable) accession number: Q9CYR6
Secondary accession number(s): B2RS40, Q543F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.