Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9CYR6 (AGM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoacetylglucosamine mutase

Short name=PAGM
EC=5.4.2.3
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase
Phosphoglucomutase-3
Short name=PGM 3
Gene names
Name:Pgm3
Synonyms:Agm1, Pgm-3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Phosphoacetylglucosamine mutase
PRO_0000148014

Sites

Active site641Phosphoserine intermediate By similarity
Metal binding641Magnesium; via phosphate group By similarity
Metal binding2761Magnesium By similarity
Metal binding2781Magnesium By similarity
Metal binding2801Magnesium By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue641Phosphoserine By similarity

Secondary structure

............. 542
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CYR6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B00E3D0F38BE4090

FASTA54259,453
        10         20         30         40         50         60 
MDLEAVCKRS ALHAKPQGLI LQYGTAGFRT NAQHLDHIMF RMGLLAVLRS KQTRSTIGVM 

        70         80         90        100        110        120 
VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLASAEEQ DVRQVLAAIV EKEAVDLTQT 

       130        140        150        160        170        180 
AFVVIARDTR PSSEKLSQSV IDGVTVLGGQ FHDYGLLTTP QLHYMVYCRN SGGRYGQATV 

       190        200        210        220        230        240 
EGYCQKLSKA FVDLTNQVSC SGDVKRSVKV DCANGIGALK LREMEHYFSR GLSVLLFNDG 

       250        260        270        280        290        300 
TQGRLNHLCG ADFVKSQQKP PQGIEMKSGE RCCSFDGDAD RIVYYYCDAD GHFHLIDGDK 

       310        320        330        340        350        360 
IATLISSFLK ELLLEIGESV NLGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA 

       370        380        390        400        410        420 
QEFDIGVYFE ANGHGTALFS EAVEVKIKRL AQELDDGKGK AARTLASIID LFNQAAGDAI 

       430        440        450        460        470        480 
SDMLVIEAIL ALKGLTVQQW DAIYVDLPNR QLKVKVADRR VISTTDAERQ AVTPPGLQEA 

       490        500        510        520        530        540 
INDLVKKYTL ARAFVRPSGT EDIVRVYAEA NSQESADRLA YEVSLLVFQL AGGIGERPQP 


TF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23381.1.
RefSeqNP_001157218.1. NM_001163746.1.
NP_082628.3. NM_028352.4.
UniGeneMm.390201.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJWNMR-A442-540[»]
ProteinModelPortalQ9CYR6.
SMRQ9CYR6. Positions 4-541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000070871.

PTM databases

PhosphoSiteQ9CYR6.

Proteomic databases

MaxQBQ9CYR6.
PaxDbQ9CYR6.
PRIDEQ9CYR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.
GeneID109785.
KEGGmmu:109785.
UCSCuc009qxm.2. mouse.

Organism-specific databases

CTD5238.
MGIMGI:97566. Pgm3.

Phylogenomic databases

eggNOGCOG1109.
GeneTreeENSGT00390000000509.
HOVERGENHBG024321.
InParanoidB2RS40.
KOK01836.
OMADIVRVYA.
OrthoDBEOG7W6WKJ.
PhylomeDBQ9CYR6.
TreeFamTF105670.

Enzyme and pathway databases

UniPathwayUPA00113; UER00530.

Gene expression databases

ArrayExpressQ9CYR6.
BgeeQ9CYR6.
CleanExMM_PGM3.
GenevestigatorQ9CYR6.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProIPR005844. 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]
PfamPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFPIRSF016408. PAGM. 1 hit.
SUPFAMSSF53738. SSF53738. 4 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9CYR6.
NextBio362755.
PROQ9CYR6.
SOURCESearch...

Entry information

Entry nameAGM1_MOUSE
AccessionPrimary (citable) accession number: Q9CYR6
Secondary accession number(s): B2RS40, Q543F9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot