Q9CYR6 (AGM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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
Short name=PGM 3

Gene names

Name:	Pgm3
Synonyms:	Agm1, Pgm-3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Inferred from mutant phenotype PubMed 17548465. Source: MGI carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro embryo development Inferred from mutant phenotype PubMed 17548465. Source: MGI glucose 1-phosphate metabolic process Inferred from direct assay PubMed 6241468PubMed 6457599. Source: MGI hemopoiesis Inferred from mutant phenotype PubMed 17548465. Source: MGI spermatogenesis Inferred from mutant phenotype PubMed 17548465. Source: MGI
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoacetylglucosamine mutase activity Inferred from mutant phenotype PubMed 17548465. Source: MGI phosphoglucomutase activity Inferred from direct assay PubMed 6241468PubMed 6457599PubMed 7323947. 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 [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] [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: 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: Melanoma.
[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

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.

IPI

IPI01023258.

RefSeq

NP_001157218.1. NM_001163746.1.
NP_082628.3. NM_028352.4.

UniGene

Mm.390201.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q9CYR6.

SMR

Q9CYR6. Positions 13-541.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000070871.

PTM databases

PhosphoSite

Q9CYR6.

Proteomic databases

PaxDb

Q9CYR6.

PRIDE

Q9CYR6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.

GeneID

109785.

KEGG

mmu:109785.

UCSC

uc009qxm.2. mouse.

Organism-specific databases

CTD

5238.

MGI

MGI:97566. Pgm3.

Phylogenomic databases

eggNOG

COG1109.

GeneTree

ENSGT00390000000509.

HOVERGEN

HBG024321.

InParanoid

B2RS40.

KO

K01836.

OMA

DIVRVYA.

OrthoDB

EOG4TMR1V.

Enzyme and pathway databases

UniPathway

UPA00113; UER00530.

Gene expression databases

ArrayExpress

Q9CYR6.

Bgee

Q9CYR6.

CleanEx

MM_PGM3.

Genevestigator

Q9CYR6.

GermOnline

ENSMUSG00000056131. Mus musculus.

Family and domain databases

Gene3D

3.40.120.10. 3 hits.

InterPro

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.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]

PANTHER

PTHR22573:SF3. PTHR22573:SF3. 1 hit.

Pfam

PF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]

PIRSF

PIRSF016408. PAGM. 1 hit.

SUPFAM

SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 4 hits.

PROSITE

PS00710. PGM_PMM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9CYR6.

NextBio

362755.

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:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program