AGM1_PIG
ID AGM1_PIG Reviewed; 542 AA.
AC F1RQM2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000303|PubMed:4996162};
DE Short=PAGM {ECO:0000305};
DE Short=PGlcNAc mutase {ECO:0000303|PubMed:4996162};
DE EC=5.4.2.3 {ECO:0000269|PubMed:468829, ECO:0000269|PubMed:4996162};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000305};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000250|UniProtKB:O95394};
DE AltName: Full=Phosphoglucomutase-3 {ECO:0000250|UniProtKB:O95394};
DE Short=PGM 3 {ECO:0000250|UniProtKB:O95394};
GN Name=PGM3 {ECO:0000250|UniProtKB:O95394};
GN Synonyms=AGM1 {ECO:0000250|UniProtKB:O95394};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Dawson H.D., Chen C.T.;
RT "Global gene expression profiling of alveolar macrophages by deep
RT sequencing.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RX PubMed=4996162; DOI=10.1016/s0021-9258(18)62155-6;
RA Fernandez-Sorensen A., Carlson D.M.;
RT "Purification and properties of phosphoacetylglucosamine mutase.";
RL J. Biol. Chem. 246:3485-3493(1971).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=468829; DOI=10.1016/s0021-9258(19)86897-7;
RA Cheng P.W., Carlson D.M.;
RT "Mechanism of phosphoacetylglucosamine mutase.";
RL J. Biol. Chem. 254:8353-8357(1979).
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:0000269|PubMed:468829, ECO:0000269|PubMed:4996162}.
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; Evidence={ECO:0000269|PubMed:468829,
CC ECO:0000269|PubMed:4996162};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:4996162};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:4996162};
CC -!- ACTIVITY REGULATION: Inhibited by Mn(2+), Cd(2+), Zn(2+), Cu(2+) and
CC Be(2+). {ECO:0000269|PubMed:4996162}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 mM for D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:4996162};
CC KM=0.39 mM for D-glucose 1-phosphate {ECO:0000269|PubMed:4996162};
CC KM=0.018 mM for fructose 1,6-diphosphate
CC {ECO:0000269|PubMed:4996162};
CC KM=0.016 mM for galactose 1,6-diphosphate
CC {ECO:0000269|PubMed:4996162};
CC KM=0.005 mM for mannose 1,6-diphosphate {ECO:0000269|PubMed:4996162};
CC KM=0.002 mM for glucose 1,6-diphosphate {ECO:0000269|PubMed:4996162};
CC Vmax=39.4 umol/min/mg enzyme for D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:4996162};
CC Vmax=28.9 umol/min/mg enzyme for D-glucose 1-phosphate
CC {ECO:0000269|PubMed:4996162};
CC Vmax=10.1 umol/min/mg enzyme for fructose 1,6-diphosphate
CC {ECO:0000269|PubMed:4996162};
CC Vmax=14.3 umol/min/mg enzyme for galactose 1,6-diphosphate
CC {ECO:0000269|PubMed:4996162};
CC Vmax=26.7 umol/min/mg enzyme for mannose 1,6-diphosphate
CC {ECO:0000269|PubMed:4996162};
CC Vmax=34.4 umol/min/mg enzyme for glucose 1,6-diphosphate
CC {ECO:0000269|PubMed:4996162};
CC pH dependence:
CC Optimum pH is 7-7.5. {ECO:0000269|PubMed:4996162};
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:0000305|PubMed:468829}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AEMK01179872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU463150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GACC01000082; JAA53725.1; -; mRNA.
DR RefSeq; XP_001924454.2; XM_001924419.4.
DR RefSeq; XP_005659464.1; XM_005659407.2.
DR AlphaFoldDB; F1RQM2; -.
DR SMR; F1RQM2; -.
DR STRING; 9823.ENSSSCP00000004806; -.
DR PaxDb; F1RQM2; -.
DR PeptideAtlas; F1RQM2; -.
DR PRIDE; F1RQM2; -.
DR Ensembl; ENSSSCT00030022007; ENSSSCP00030009944; ENSSSCG00030015873.
DR Ensembl; ENSSSCT00035094807; ENSSSCP00035039836; ENSSSCG00035070159.
DR Ensembl; ENSSSCT00045016316; ENSSSCP00045011275; ENSSSCG00045009611.
DR Ensembl; ENSSSCT00050021173; ENSSSCP00050008843; ENSSSCG00050015639.
DR Ensembl; ENSSSCT00055030841; ENSSSCP00055024560; ENSSSCG00055015625.
DR Ensembl; ENSSSCT00065069324; ENSSSCP00065030198; ENSSSCG00065050601.
DR Ensembl; ENSSSCT00070043212; ENSSSCP00070036361; ENSSSCG00070021741.
DR GeneID; 100156015; -.
DR KEGG; ssc:100156015; -.
DR CTD; 5238; -.
DR eggNOG; KOG2537; Eukaryota.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; F1RQM2; -.
DR OrthoDB; 345441at2759; -.
DR TreeFam; TF105670; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 1.
DR Genevisible; F1RQM2; SS.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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 Acetylation; Carbohydrate metabolism; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..542
FT /note="Phosphoacetylglucosamine mutase"
FT /id="PRO_0000431296"
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:0000250|UniProtKB:O95394"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95394"
SQ SEQUENCE 542 AA; 59474 MW; A5C7A8492751E150 CRC64;
MDLDAITKHS ASHAKPDGLI LQYGTAGFRT KADRLDHVMF RMGLLAVLRS KQTKSTIGVM
VTASHNPEDD NGVKLVDPLG EMLAPSWEEH ATHLANAEEQ DLARALVAIS EEAAVNLHQD
AFVVIGRDTR PSSEKLSESV IDGVTVLGGQ FHDYGLLTTP QLHYMVCCRN TGGQYGEATI
DGYYHKLSTA FVELSKQASC SGDDHRTLKV DCANGIGALK LKEMKHYLPQ GLSVQLFNDG
TKGKLNHFCG ADFVKSHQKP PEGIEMKANE RCCSFDGDAD RIIYYYCDVD GHFHLIDGDK
IATLISSFLK ELLLEIGESL TVGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA
QEFDLGVYFE ANGHGTVLFS KAAEAKIRQL AKELEDKKGK AAKMLENVID LFNQATGDAI
SDMLVIEAIL ALKGLTIQQW DALYTDLPNR QLKVKVADRQ VISTTDAERQ VVKPPGLQEA
INDLVKKYKL SRAFVRPSGT EDVVRVYAEA DSQENADSLA YEVSLAVFQQ AGGVGERPQP
GF
