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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Phosphoserine intermediateBy similarity
Metal bindingi64 – 641Magnesium; via phosphate groupBy similarity
Metal bindingi276 – 2761MagnesiumBy similarity
Metal bindingi278 – 2781MagnesiumBy similarity
Metal bindingi280 – 2801MagnesiumBy similarity
Binding sitei505 – 5051SubstrateBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphoacetylglucosamine mutase activity Source: UniProtKB
  3. phosphoglucomutase activity Source: MGI

GO - Biological processi

  1. glucose 1-phosphate metabolic process Source: MGI
  2. hemopoiesis Source: MGI
  3. protein N-linked glycosylation Source: UniProtKB
  4. protein O-linked glycosylation Source: UniProtKB
  5. spermatogenesis Source: MGI
  6. 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

ReactomeiREACT_284517. 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
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97566. Pgm3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Phosphoacetylglucosamine mutasePRO_0000148014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei62 – 621PhosphothreonineBy similarity
Modified residuei64 – 641PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CYR6.
PaxDbiQ9CYR6.
PRIDEiQ9CYR6.

PTM databases

PhosphoSiteiQ9CYR6.

Expressioni

Gene expression databases

BgeeiQ9CYR6.
CleanExiMM_PGM3.
ExpressionAtlasiQ9CYR6. baseline and differential.
GenevestigatoriQ9CYR6.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070871.

Structurei

Secondary structure

1
542
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi449 – 4546Combined sources
Beta strandi459 – 4624Combined sources
Beta strandi470 – 4745Combined sources
Helixi477 – 48711Combined sources
Beta strandi488 – 4969Combined sources
Beta strandi498 – 51215Combined sources
Helixi513 – 53018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJWNMR-A442-540[»]
ProteinModelPortaliQ9CYR6.
SMRiQ9CYR6. Positions 4-541.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CYR6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3723Substrate bindingBy similarity
Regioni496 – 5005Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
GeneTreeiENSGT00390000000509.
HOVERGENiHBG024321.
InParanoidiQ9CYR6.
KOiK01836.
OMAiKPNERCC.
OrthoDBiEOG7W6WKJ.
PhylomeDBiQ9CYR6.
TreeFamiTF105670.

Family and domain databases

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.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJWNMR-A442-540[»]
ProteinModelPortaliQ9CYR6.
SMRiQ9CYR6. Positions 4-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070871.

PTM databases

PhosphoSiteiQ9CYR6.

Proteomic databases

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

eggNOGiCOG1109.
GeneTreeiENSGT00390000000509.
HOVERGENiHBG024321.
InParanoidiQ9CYR6.
KOiK01836.
OMAiKPNERCC.
OrthoDBiEOG7W6WKJ.
PhylomeDBiQ9CYR6.
TreeFamiTF105670.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00530.
ReactomeiREACT_284517. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

EvolutionaryTraceiQ9CYR6.
NextBioi362755.
PROiQ9CYR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CYR6.
CleanExiMM_PGM3.
ExpressionAtlasiQ9CYR6. baseline and differential.
GenevestigatoriQ9CYR6.

Family and domain databases

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.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum, Embryo, Heart, Kidney, Placenta, Spinal ganglion and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Solution structure of the C-terminal domain of mouse phosphoacetylglucosamine mutase (PAGM)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 442-540.

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: April 1, 2015
This is version 124 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

External Data

Dasty 3

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 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.