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Q9CYR6

- AGM1_MOUSE

UniProt

Q9CYR6 - AGM1_MOUSE

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Protein
Phosphoacetylglucosamine mutase
Gene
Pgm3, Agm1, Pgm-3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Interconverts GlcNAc-6-P and GlcNAc-1-P By similarity.

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Phosphoserine intermediate By similarity
Metal bindingi64 – 641Magnesium; via phosphate group By similarity
Metal bindingi276 – 2761Magnesium By similarity
Metal bindingi278 – 2781Magnesium By similarity
Metal bindingi280 – 2801Magnesium By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. UDP-N-acetylglucosamine biosynthetic process Source: MGI
  2. carbohydrate metabolic process Source: InterPro
  3. glucose 1-phosphate metabolic process Source: MGI
  4. hemopoiesis Source: MGI
  5. spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198714. Synthesis of UDP-N-acetyl-glucosamine.
UniPathwayiUPA00113; UER00530.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoacetylglucosamine mutase (EC:5.4.2.3)
Short name:
PAGM
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase
Phosphoglucomutase-3
Short name:
PGM 3
Gene namesi
Name:Pgm3
Synonyms:Agm1, Pgm-3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:97566. Pgm3.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Phosphoacetylglucosamine mutase
PRO_0000148014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei64 – 641Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CYR6.
PaxDbiQ9CYR6.
PRIDEiQ9CYR6.

PTM databases

PhosphoSiteiQ9CYR6.

Expressioni

Gene expression databases

ArrayExpressiQ9CYR6.
BgeeiQ9CYR6.
CleanExiMM_PGM3.
GenevestigatoriQ9CYR6.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070871.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJWNMR-A442-540[»]
ProteinModelPortaliQ9CYR6.
SMRiQ9CYR6. Positions 4-541.

Miscellaneous databases

EvolutionaryTraceiQ9CYR6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1109.
GeneTreeiENSGT00390000000509.
HOVERGENiHBG024321.
InParanoidiB2RS40.
KOiK01836.
OMAiDIVRVYA.
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

MDLEAVCKRS ALHAKPQGLI LQYGTAGFRT NAQHLDHIMF RMGLLAVLRS    50
KQTRSTIGVM VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLASAEEQ 100
DVRQVLAAIV EKEAVDLTQT AFVVIARDTR PSSEKLSQSV IDGVTVLGGQ 150
FHDYGLLTTP QLHYMVYCRN SGGRYGQATV EGYCQKLSKA FVDLTNQVSC 200
SGDVKRSVKV DCANGIGALK LREMEHYFSR GLSVLLFNDG TQGRLNHLCG 250
ADFVKSQQKP PQGIEMKSGE RCCSFDGDAD RIVYYYCDAD GHFHLIDGDK 300
IATLISSFLK ELLLEIGESV NLGVVQTAYA NGSSTRYLEE VMKVPVYCTK 350
TGVKHLHHKA QEFDIGVYFE ANGHGTALFS EAVEVKIKRL AQELDDGKGK 400
AARTLASIID LFNQAAGDAI SDMLVIEAIL ALKGLTVQQW DAIYVDLPNR 450
QLKVKVADRR VISTTDAERQ AVTPPGLQEA INDLVKKYTL ARAFVRPSGT 500
EDIVRVYAEA NSQESADRLA YEVSLLVFQL AGGIGERPQP TF 542
Length:542
Mass (Da):59,453
Last modified:June 1, 2001 - v1
Checksum:iB00E3D0F38BE4090
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS23381.1.
RefSeqi NP_001157218.1. NM_001163746.1.
NP_082628.3. NM_028352.4.
UniGenei Mm.390201.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WJW NMR - A 442-540 [» ]
ProteinModelPortali Q9CYR6.
SMRi Q9CYR6. Positions 4-541.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000070871.

PTM databases

PhosphoSitei Q9CYR6.

Proteomic databases

MaxQBi Q9CYR6.
PaxDbi Q9CYR6.
PRIDEi Q9CYR6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000070064 ; ENSMUSP00000070871 ; ENSMUSG00000056131 .
GeneIDi 109785.
KEGGi mmu:109785.
UCSCi uc009qxm.2. mouse.

Organism-specific databases

CTDi 5238.
MGIi MGI:97566. Pgm3.

Phylogenomic databases

eggNOGi COG1109.
GeneTreei ENSGT00390000000509.
HOVERGENi HBG024321.
InParanoidi B2RS40.
KOi K01836.
OMAi DIVRVYA.
OrthoDBi EOG7W6WKJ.
PhylomeDBi Q9CYR6.
TreeFami TF105670.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00530 .
Reactomei REACT_198714. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

EvolutionaryTracei Q9CYR6.
NextBioi 362755.
PROi Q9CYR6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9CYR6.
Bgeei Q9CYR6.
CleanExi MM_PGM3.
Genevestigatori Q9CYR6.

Family and domain databases

Gene3Di 3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProi IPR005844. 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 ]
Pfami PF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view ]
PIRSFi PIRSF016408. PAGM. 1 hit.
SUPFAMi SSF53738. SSF53738. 4 hits.
SSF55957. SSF55957. 1 hit.
PROSITEi PS00710. PGM_PMM. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 117 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

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