ID A0A0D1YH65_9EURO Unreviewed; 568 AA.
AC A0A0D1YH65;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=PV11_07829 {ECO:0000313|EMBL:KIV80319.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV80319.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV80319.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV80319.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN846953; KIV80319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YH65; -.
DR STRING; 1016849.A0A0D1YH65; -.
DR OrthoDB; 1475at2759; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000053599; 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; 3.
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:UP000053599}.
FT DOMAIN 74..111
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 139..199
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..317
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21405"
FT DOMAIN 331..470
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 487..563
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 88
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 406..408
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 531..535
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ SEQUENCE 568 AA; 62443 MW; 29ED7C5A03E20625 CRC64;
MSSYSNPRES VFNQPKPVVT LPSDLLDAVT KNVEPYPIPE GRRYEYGTAG FRMKANAGLD
HVIYTVGLTA AARSKKRNAT IGIMITASHN PAEDNGVKLV DPMGDMLEQS WESYATTLAN
TPNDKLAKAY ENLVNETLVD EIRQLHERPA KVIFARDTRA SGPYLVTALK AALDAVKVEY
TDYGLLTTPQ LHYIVRCVNT LNSPYAFGEP TEQGYYEKMA KAFKTLMYGR SIHGSVTVDC
ANGVGGPKLK EMIKYLPSGK EGGIDIRIIN DDVVRPESLN LDCGADYVKT KQRAPPSSNA
GPGDRCCSLD GDADRIVYYY TDESKTFHLL DGDRIATLGA VFLADMTRVA GIDSKLKIGI
IQTAYANGAA TEYVEKVLKL PVAVTPTGVK HLHHAAARYD IGVYFEANGH GTVLFSDNAI
KVIKESEPKS PGQKHALDSL RACIDLINQA VGDAISDMLF AEVVLAHKSW TLENWRNTYI
DLPNRLVRVE VRDRSIFKTT DAERKLESPK GAQDEIDKFC QMYVKGRAFA RASGTEDAVR
VYAEAHSKTE AEKLAGQVAE VVRKYGAN
//
