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Database: UniProt
Entry: A0A022QYM8_ERYGU
LinkDB: A0A022QYM8_ERYGU
Original site: A0A022QYM8_ERYGU 
ID   A0A022QYM8_ERYGU        Unreviewed;       551 AA.
AC   A0A022QYM8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00012731, ECO:0000256|PIRNR:PIRNR016408};
DE            Short=PAGM {ECO:0000256|PIRNR:PIRNR016408};
DE            EC=5.4.2.3 {ECO:0000256|ARBA:ARBA00012731, ECO:0000256|PIRNR:PIRNR016408};
DE   AltName: Full=Acetylglucosamine phosphomutase {ECO:0000256|ARBA:ARBA00032065, ECO:0000256|PIRNR:PIRNR016408};
DE   AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|ARBA:ARBA00031926, ECO:0000256|PIRNR:PIRNR016408};
GN   ORFNames=MIMGU_mgv1a003986mg {ECO:0000313|EMBL:EYU33036.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU33036.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU33036.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- FUNCTION: Interconverts GlcNAc-6-P and GlcNAc-1-P.
CC       {ECO:0000256|PIRNR:PIRNR016408}.
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:0000256|ARBA:ARBA00000558,
CC         ECO:0000256|PIRNR:PIRNR016408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016408,
CC         ECO:0000256|PIRSR:PIRSR016408-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR016408,
CC       ECO:0000256|PIRSR:PIRSR016408-3};
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:0000256|ARBA:ARBA00004865, ECO:0000256|PIRNR:PIRNR016408}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|PIRNR:PIRNR016408}.
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DR   EMBL; KI630795; EYU33036.1; -; Genomic_DNA.
DR   RefSeq; XP_012842635.1; XM_012987181.1.
DR   AlphaFoldDB; A0A022QYM8; -.
DR   STRING; 4155.A0A022QYM8; -.
DR   GeneID; 105962843; -.
DR   KEGG; egt:105962843; -.
DR   eggNOG; KOG2537; Eukaryota.
DR   OMA; WEAYATK; -.
DR   OrthoDB; 1475at2759; -.
DR   PhylomeDB; A0A022QYM8; -.
DR   UniPathway; UPA00113; UER00530.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR   CDD; cd03086; PGM3; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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; IPR049023; AMG1_II.
DR   InterPro; IPR049022; AMG1_III.
DR   InterPro; IPR016657; PAGM.
DR   PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   Pfam; PF21405; AMG1_II; 1.
DR   Pfam; PF21404; AMG1_III; 1.
DR   Pfam; PF02878; PGM_PMM_I; 2.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PIRSF; PIRSF016408; PAGM; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR016408};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR016408};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR016408};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT   DOMAIN          58..87
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          125..177
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          182..289
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21405"
FT   DOMAIN          304..453
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21404"
FT   DOMAIN          495..542
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   ACT_SITE        67
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         284
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         383..385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT   BINDING         514..518
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT   BINDING         523
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ   SEQUENCE   551 AA;  59515 MW;  A8AD1349BDD35D7E CRC64;
     MNQQQRSALL HSSSLFPPPP GVKLSYGTAG FRADASLLES TVFRVGILAA LRSIQTGSVI
     GLMITASHNQ VSDNGVKIAD PSGGMLTQLW EPFADAIANA PDPHSLLQLL DDFVKKENIT
     LEGGPAARVL LGRDTRPSGA SLVEAAKQGI TCITGATAID VGVLTTPQLH WMVRAKNKGV
     EASEHHYYDQ IVTSFSYLMD NIPRENSSKD VNDKLIVDGA DGVGGEKLEK LKSSLKYLSI
     DVRNYGDGVL NEGVGADYVQ KEKVVPRGFG PSDAGIRCAS LDGDADRLVY FSVLSNSNKI
     DLVDGDKILS LFALFLKEQL RILDDKANTS SYKASLGVVQ TAYANGASTE YLKQLGLEVV
     LTPTGVKYLH EKAAEYDIGI YFEANGHGTI LFSETFLSWL ENINNELSST SKGSDQHKAA
     SNLLAVSKLI NQAVGDALSG LLLVEAILQH MGWSIKKWNE LYQDLPSRQL KVKVVDRTAV
     ITGNAETVVV SPVGIQEAID AEIAKYTKGR CFVRPSGTED VVRVYAEAST QEAADSLAHS
     VMVIVHQFLW F
//
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