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Database: UniProt
Entry: W9C1B9_SCLBF
LinkDB: W9C1B9_SCLBF
Original site: W9C1B9_SCLBF 
ID   W9C1B9_SCLBF            Unreviewed;       538 AA.
AC   W9C1B9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=SBOR_9025 {ECO:0000313|EMBL:ESZ90592.1};
OS   Sclerotinia borealis (strain F-4128).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ90592.1, ECO:0000313|Proteomes:UP000019487};
RN   [1] {ECO:0000313|EMBL:ESZ90592.1, ECO:0000313|Proteomes:UP000019487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX   PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT   "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT   pathogenic fungus.";
RL   Genome Announc. 2:E0117513-E0117513(2014).
CC   -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC       the synthesis of uridine diphosphate/UDP-GlcNAc, which is a
CC       biosynthetic precursor of chitin and also supplies the amino sugars for
CC       N-linked oligosaccharides of glycoproteins.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESZ90592.1}.
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DR   EMBL; AYSA01000602; ESZ90592.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9C1B9; -.
DR   STRING; 1432307.W9C1B9; -.
DR   HOGENOM; CLU_022890_1_0_1; -.
DR   OrthoDB; 1475at2759; -.
DR   UniPathway; UPA00113; UER00530.
DR   Proteomes; UP000019487; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03086; PGM3; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2.
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; IPR016066; A-D-PHexomutase_CS.
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; 4.
DR   PROSITE; PS00710; PGM_PMM; 1.
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:UP000019487}.
FT   DOMAIN          56..87
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          119..172
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          203..285
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21405"
FT   DOMAIN          299..438
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21404"
FT   DOMAIN          454..530
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   ACT_SITE        64
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         278
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         374..376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT   BINDING         499..503
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT   BINDING         508
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ   SEQUENCE   538 AA;  58826 MW;  628F50047D38913D CRC64;
     MDSRILEASN KHPKPAHRVF QYGTAGFRMK ATLLDSVVFR VGLVAALRSR KLGGQTIGVM
     ITASHNPPED NGVKLVDPMG EMLENSWEAY STQLANAKSE DVVQVYRKLE KDLKINPETP
     ARVIYARDTR PSGPRLVAAL VDALEATGTD YTDFKLLTTP QLHYLTRCTN TEGTPQAYGD
     VSEVGYYEKL AKAFVRAMKG KKTFGSVTVD CANGVGGPKL HELIKYLPKG ILNIKVINDD
     VIRPERLNHD CGADFVKTKQ RAPPSSRAGT NDRCCSLDGD ADRIIYYFND PDLGFRLLDG
     DRIATLAASF ITDLAKDAGL ADELRIGVVQ TAYANGASTK YVEKTLKLPV VCTPTGVKWL
     HHAATKFDVG VYFEANGHGT VVFSQQALKA VTSTEPESPA QASALEALRA LTDLINQTVG
     DALSDMLLVE TILAHKSWTP KEWDQTYVDL PNRLVRVEVN DRNVFKTTDA ERKLLEPQGT
     QTQIDALVAK FKDGRSFARA SGTEDALRVY AEAATRSEAD DLATKVASLC KIEGSIKG
//
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