AGM1_MOUSE
ID AGM1_MOUSE Reviewed; 542 AA.
AC Q9CYR6; B2RS40; Q543F9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000305};
DE Short=PAGM;
DE EC=5.4.2.3 {ECO:0000250|UniProtKB:O95394};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000305};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000305};
DE AltName: Full=Phosphoglucomutase-3 {ECO:0000312|MGI:MGI:97566};
DE Short=PGM 3;
GN Name=Pgm3 {ECO:0000312|MGI:MGI:97566}; Synonyms=Agm1, Pgm-3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Embryo, Heart, Kidney, Placenta, Spinal ganglion, and
RC Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP STRUCTURE BY NMR OF 442-540.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal domain of mouse
RT phosphoacetylglucosamine mutase (PAGM).";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide
CC critical to multiple glycosylation pathways including protein N- and O-
CC glycosylation. {ECO:0000250|UniProtKB:O95394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513,
CC ChEBI:CHEBI:57776; EC=5.4.2.3;
CC Evidence={ECO:0000250|UniProtKB:O95394};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9P4V2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC {ECO:0000250|UniProtKB:O95394}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AK013402; BAB28834.1; -; mRNA.
DR EMBL; AK028066; BAC25733.1; -; mRNA.
DR EMBL; AK049337; BAC33692.1; -; mRNA.
DR EMBL; AK051706; BAC34728.1; -; mRNA.
DR EMBL; AK160913; BAE36087.1; -; mRNA.
DR EMBL; AK165513; BAE38229.1; -; mRNA.
DR EMBL; AK169082; BAE40866.1; -; mRNA.
DR EMBL; AK169787; BAE41366.1; -; mRNA.
DR EMBL; BC138700; AAI38701.1; -; mRNA.
DR CCDS; CCDS23381.1; -.
DR RefSeq; NP_001157218.1; NM_001163746.1.
DR RefSeq; NP_082628.3; NM_028352.4.
DR PDB; 1WJW; NMR; -; A=442-540.
DR PDBsum; 1WJW; -.
DR AlphaFoldDB; Q9CYR6; -.
DR BMRB; Q9CYR6; -.
DR SMR; Q9CYR6; -.
DR BioGRID; 225039; 3.
DR STRING; 10090.ENSMUSP00000070871; -.
DR iPTMnet; Q9CYR6; -.
DR PhosphoSitePlus; Q9CYR6; -.
DR EPD; Q9CYR6; -.
DR jPOST; Q9CYR6; -.
DR MaxQB; Q9CYR6; -.
DR PaxDb; Q9CYR6; -.
DR PRIDE; Q9CYR6; -.
DR ProteomicsDB; 285566; -.
DR Antibodypedia; 31667; 279 antibodies from 24 providers.
DR DNASU; 109785; -.
DR Ensembl; ENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.
DR GeneID; 109785; -.
DR KEGG; mmu:109785; -.
DR UCSC; uc009qxm.2; mouse.
DR CTD; 5238; -.
DR MGI; MGI:97566; Pgm3.
DR VEuPathDB; HostDB:ENSMUSG00000056131; -.
DR eggNOG; KOG2537; Eukaryota.
DR GeneTree; ENSGT00390000000509; -.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; Q9CYR6; -.
DR OMA; WEAYATK; -.
DR OrthoDB; 345441at2759; -.
DR PhylomeDB; Q9CYR6; -.
DR TreeFam; TF105670; -.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00530.
DR BioGRID-ORCS; 109785; 24 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q9CYR6; -.
DR PRO; PR:Q9CYR6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CYR6; protein.
DR Bgee; ENSMUSG00000056131; Expressed in epithelium of small intestine and 224 other tissues.
DR ExpressionAtlas; Q9CYR6; baseline and differential.
DR Genevisible; Q9CYR6; MM.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IMP:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:MGI.
DR CDD; cd03086; PGM3; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR016657; PAGM.
DR Pfam; PF02878; PGM_PMM_I; 2.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PIRSF; PIRSF016408; PAGM; 1.
DR SUPFAM; SSF53738; SSF53738; 4.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..542
FT /note="Phosphoacetylglucosamine mutase"
FT /id="PRO_0000148014"
FT ACT_SITE 64
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 370..372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 496..500
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95394"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:1WJW"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:1WJW"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:1WJW"
FT HELIX 477..487
FT /evidence="ECO:0007829|PDB:1WJW"
FT STRAND 488..496
FT /evidence="ECO:0007829|PDB:1WJW"
FT STRAND 498..512
FT /evidence="ECO:0007829|PDB:1WJW"
FT HELIX 513..530
FT /evidence="ECO:0007829|PDB:1WJW"
SQ SEQUENCE 542 AA; 59453 MW; B00E3D0F38BE4090 CRC64;
MDLEAVCKRS ALHAKPQGLI LQYGTAGFRT NAQHLDHIMF RMGLLAVLRS KQTRSTIGVM
VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLASAEEQ DVRQVLAAIV EKEAVDLTQT
AFVVIARDTR PSSEKLSQSV IDGVTVLGGQ FHDYGLLTTP QLHYMVYCRN SGGRYGQATV
EGYCQKLSKA FVDLTNQVSC SGDVKRSVKV DCANGIGALK LREMEHYFSR GLSVLLFNDG
TQGRLNHLCG ADFVKSQQKP PQGIEMKSGE RCCSFDGDAD RIVYYYCDAD GHFHLIDGDK
IATLISSFLK ELLLEIGESV NLGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA
QEFDIGVYFE ANGHGTALFS EAVEVKIKRL AQELDDGKGK AARTLASIID LFNQAAGDAI
SDMLVIEAIL ALKGLTVQQW DAIYVDLPNR QLKVKVADRR VISTTDAERQ AVTPPGLQEA
INDLVKKYTL ARAFVRPSGT EDIVRVYAEA NSQESADRLA YEVSLLVFQL AGGIGERPQP
TF
