ID A0A7K5XGI9_9CHAR Unreviewed; 541 AA.
AC A0A7K5XGI9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00070218};
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};
DE AltName: Full=Phosphoglucomutase-3 {ECO:0000256|ARBA:ARBA00081059};
DE Flags: Fragment;
GN Name=Pgm3 {ECO:0000313|EMBL:NWU51776.1};
GN ORFNames=DROARD_R04033 {ECO:0000313|EMBL:NWU51776.1};
OS Dromas ardeola.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Dromadidae;
OC Dromas.
OX NCBI_TaxID=458190 {ECO:0000313|EMBL:NWU51776.1, ECO:0000313|Proteomes:UP000586671};
RN [1] {ECO:0000313|EMBL:NWU51776.1, ECO:0000313|Proteomes:UP000586671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-012-55 {ECO:0000313|EMBL:NWU51776.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWU51776.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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, a sugar nucleotide
CC critical to multiple glycosylation pathways including protein N- and O-
CC glycosylation. {ECO:0000256|ARBA:ARBA00060228}.
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|PIRSR:PIRSR016408-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {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}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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:NWU51776.1}.
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DR EMBL; VYZM01010045; NWU51776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K5XGI9; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000586671; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030097; P:hemopoiesis; IEA:TreeGrafter.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03086; PGM3; 1.
DR FunFam; 3.30.310.50:FF:000003; Phosphoacetylglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000013; Phosphoacetylglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000015; Phosphoacetylglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000019; Phosphoacetylglucosamine mutase; 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; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR016408-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR016408-3};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000586671}.
FT DOMAIN 52..100
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 103..166
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 178..283
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21405"
FT DOMAIN 297..435
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 452..525
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT COILED 388..415
FT /evidence="ECO:0000256|SAM:Coils"
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 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 370..372
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 497..501
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWU51776.1"
FT NON_TER 541
FT /evidence="ECO:0000313|EMBL:NWU51776.1"
SQ SEQUENCE 541 AA; 59936 MW; 73803B7183C85A37 CRC64;
MDTEALKKYS ALHPKPAGLT LQYGTAGFRT KAEQLDHVMF RMGLLAVLRS KAMASTIGIM
VTASHNPEED NGVKLVDPLG EMLHPSWEEY ATQLANAEEQ ELQKIITEIC QKAAVNQDKD
ASVFIGRDTR PSSKKLSQSV IDGISVLGGQ YHDYGLVTTP QLHYMVCCQN TQGQYGKATL
EGYYEKLSKA FTELIKRSPS SGESQRHLKI DCANGIGALK LSEMQPYFPK EVQIHLYNDG
TKEKLNHLCG ADFVKVHQKP PRGLAMKPNE RCCSFDGDAD RIVYYYKDAT GHFHLIDGDK
IATLISIFLK ELLAKLGQTL KMAVVQTAYA NGSSTRYLEE TLKVPVHCVK TGVKHLHHKA
QEFDVGVYFE ANGHGTVLFS KVAETKIRQL AKEEKDDEKR EAAKVLENMI DLINQTVGDA
VSDMLVIEAI LALKGLTVQQ WDAIYTDLPN RLLKVQVADR RVIDTTDAER RAVTPPGLQE
KIDALVKNYK LSRAFVRPSG TEDVVRIYAE ADTQENADAL AHEVSLAVYH LAGGKGAPPQ
P
//
