Reviewed, UniProtKB/Swiss-Prot Q9CYR6 (AGM1_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphoacetylglucosamine mutase
      Short name=PAGM
    EC=5.4.2.3
Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
    Phosphoglucomutase 3

Gene names

Name:	Pgm3
Synonyms:	Agm1, Pgm-3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	UDP-N-acetylglucosamine biosynthetic process Inferred from mutant phenotype. Source: MGI embryonic development Inferred from mutant phenotype. Source: MGI glucose 1-phosphate metabolic process Inferred from direct assay. Source: MGI hemopoiesis Inferred from mutant phenotype. Source: MGI spermatogenesis Inferred from mutant phenotype. Source: MGI
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoacetylglucosamine mutase activity Inferred from mutant phenotype. Source: MGI phosphoglucomutase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 542

542

Phosphoacetylglucosamine mutase

PRO_0000148014

Sites

Active site

64

1

Phosphoserine intermediate By similarity

Metal binding

64

1

Magnesium; via phosphate group By similarity

Metal binding

276

1

Magnesium By similarity

Metal binding

278

1

Magnesium By similarity

Metal binding

280

1

Magnesium By similarity

Amino acid modifications

Modified residue

64

1

Phosphoserine Ref.3 Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

542

Helix Strand Turn

Details...

Beta strand

449 – 454

6

Beta strand

459 – 462

4

Beta strand

470 – 474

5

Helix

477 – 487

11

Beta strand

488 – 496

9

Beta strand

498 – 512

15

Helix

513 – 530

18

Sequences

	Sequence		Length	Mass (Da)
	Q9CYR6-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B00E3D0F38BE4090	FASTA	542	59,453
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [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: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
[5]	"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

EMBLGenBankDDBJ

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.

IPI

IPI00318898.

RefSeq

NP_001157218.1.
NP_082628.3.

UniGene

Mm.390201

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WJW	NMR	-	A	442-540	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9CYR6.

PTM databases

PhosphoSite

Q9CYR6.

Proteomic databases

PRIDE

Q9CYR6.

Genome annotation databases

Ensembl

ENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131; Mus musculus. [Genome view]

GeneID

109785.

Organism-specific databases

MGI

MGI:97566. Pgm3.

Phylogenomic databases

HOVERGEN

Q9CYR6.

OMA

MLVIEAI.

Enzyme and pathway databases

BRENDA

5.4.2.3. 244.

Gene expression databases

ArrayExpress

Q9CYR6.

Bgee

Q9CYR6.

CleanEx

MM_PGM3.

Genevestigator

Q9CYR6.

GermOnline

ENSMUSG00000056131. Mus musculus.

Family and domain databases

InterPro

IPR005844. 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]

Gene3D

G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 1 hit.

Pfam

PF02878. PGM_PMM_I. 2 hits.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]

PIRSF

PIRSF016408. PAGM. 1 hit.

PROSITE

PS00710. PGM_PMM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

AGM1_MOUSE

Accession

Primary (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:	November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)