ID A0A5C6NQS1_9TELE Unreviewed; 545 AA.
AC A0A5C6NQS1;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00070218, 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|PIRNR:PIRNR016408};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|PIRNR:PIRNR016408};
GN ORFNames=D4764_19G0007870 {ECO:0000313|EMBL:TWW68989.1};
OS Takifugu flavidus (sansaifugu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW68989.1, ECO:0000313|Proteomes:UP000324091};
RN [1] {ECO:0000313|EMBL:TWW68989.1, ECO:0000313|Proteomes:UP000324091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW68989.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TWW68989.1};
RA Xiao S.;
RT "Chromosome genome assembly for Takifugu flavidus.";
RL Submitted (APR-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 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:TWW68989.1}.
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DR EMBL; RHFK02000011; TWW68989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6NQS1; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000324091; Chromosome 19.
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:0030097; P:hemopoiesis; IEA:TreeGrafter.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniRule.
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; 3.
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 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000324091}.
FT DOMAIN 52..89
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 114..173
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 193..284
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21405"
FT DOMAIN 298..437
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 455..527
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 65
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 371..373
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 545 AA; 59889 MW; 8E9BB33AB59297E4 CRC64;
MSPFEDVYEE SKFHPKLEGL LLPYGTAGFR SNANHLDHIM FRMGLLAVLR SQNTKATIGV
MVTASHNPEE DNGVKIIDPM GEMMSTSWEG YATQLANAEQ EDLIDALKEI IEKEAIDLSL
EAKVFLGKDT RKSGVKLSEA VISGVSALGG HSKDFGLVTT PQLHYAVRCQ NTKGKYGEPS
VEGYNKKLSA AFIQLTNNAF NCTDDQKHLS VDGANGIGAL KLREIECHLK KSAHITLFND
GSKRKLNDQC GADFVKVHQK APIGIEINPG ERGCSFDGDA DRIVYYYTDS QRRFHLLDGD
KIATLISIFL KELLTQSGLN LTMAVVQTAY ANGSSTDYLR DTLKVTVQCS KTGVKYLQEM
AQKFDIGVYF EANGHGTVVF SKSAEDQIHQ LAEDPSANDE AKRAARMLQS SVNVINQTIG
DAISDMLLIE AILAIKGMTI QQWHAIYTDL PNRQIKVKVA DRRVIDTTDA ERRAVSPAGL
QEAIDSLVKR HKKARSFVRP SGTEDVVRIY AEAETQESAD ALAHEVSLAV YRLAGGVGDE
PKPLH
//
