ID A0A3F3PYD3_9EURO Unreviewed; 430 AA.
AC A0A3F3PYD3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00012731};
DE EC=5.4.2.3 {ECO:0000256|ARBA:ARBA00012731};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000256|ARBA:ARBA00032065};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|ARBA:ARBA00031926};
GN ORFNames=BDQ94DRAFT_52885 {ECO:0000313|EMBL:RDH31895.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH31895.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH31895.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH31895.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; KZ852052; RDH31895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PYD3; -.
DR STRING; 1341132.A0A3F3PYD3; -.
DR OrthoDB; 1475at2759; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 5..54
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 66..172
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21405"
FT DOMAIN 186..325
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 341..418
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 430 AA; 46891 MW; 6A4CCC1E2C078234 CRC64;
MENPARVVFA RDTRASGSRL VSVINAALTA SEVEFLDLKY MTTPQLHYVV RCKNTLGTQY
EYGEPTEQGY YEKLAEAFKR VMRGVKVKGS LTVDCANGVG GPKLRELIKY LPGPEEGGMD
IKIVNDDVIN PDSLNFECGA DYVKTKQRAP PSSKAAALDR CASLDGDADR IVYYFIDESN
TFRLLDGDRI ATLAASFIGD LARSAGIAQK LKIGVVQTAY ANGSSTDYIE KVLKLPSVCT
NTGVKHLHHA ALRFDVGVYF EANGHGTITF SETALKTIKN TEPQSPAQQR SLECLQALTD
LINQAVGDAI SDMLLVEAIL AHKGWSPKEW LATYTDLPSR LVRVEVADRS IFKAYDAERK
LESPAGLQAK IESLQSRYNK GRSFARASGT EDAVRVYAEA ASRSEADDLA TRVANAVREA
GTAKETLQSA
//
