ID A0A078HKT9_BRANA Unreviewed; 545 AA.
AC A0A078HKT9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 Name=BnaA10g16760D {ECO:0000313|EMBL:CDY38482.1};
GN ORFNames=GSBRNA2T00065929001 {ECO:0000313|EMBL:CDY38482.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY38482.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY38482.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- FUNCTION: Interconverts GlcNAc-6-P and GlcNAc-1-P.
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; LK032424; CDY38482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078HKT9; -.
DR STRING; 3708.A0A078HKT9; -.
DR PaxDb; 3708-A0A078HKT9; -.
DR EnsemblPlants; CDY38482; CDY38482; GSBRNA2T00065929001.
DR Gramene; CDY38482; CDY38482; GSBRNA2T00065929001.
DR OMA; KKCRLGV; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR CDD; cd03086; PGM3; 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; IPR049023; AMG1_II.
DR InterPro; IPR049022; AMG1_III.
DR InterPro; IPR016657; PAGM.
DR PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR PANTHER; PTHR45955:SF2; 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.
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:UP000028999}.
FT DOMAIN 59..92
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 115..176
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 181..286
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21405"
FT DOMAIN 304..446
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 464..539
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 68
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
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 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 379..381
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 507..511
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 516
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ SEQUENCE 545 AA; 59010 MW; C3C64E179EF9AD00 CRC64;
MEETQIASIL KTSELYPIPQ SIKLSYGTAG FRADASLLES TVYRVGILSS LRSLKLNSST
VGLMITASHN KVSDNGVKVS DPSGGMLSQE WEPFADQIAN ASSPKELVSL IKDFVEKKEI
AIEKGGEVWL GRDTRLSGES LLRAAEIGVR SVLGSVAVDV GVLTTPQLHW MVRAKNKGLN
ATESDYFENL ITSFKCLIGL IPVKLESSKL VLDGANGVGG LKMEVLIRSL SDIDVEIRNT
GRDGGVLNEG VGADFVQKEK VVPLGFGLKD VGMRCASFDG DADRLVYFYI PSESCGGDKV
ELLDGDKILS LFALFIKEQL NIIGDEGKKC RLGVVQTAYA NGASTDYVKE MGLEVVFAKT
GVKHLHEKAE EFDVGIYFEA NGHGTILFSE CFLSWLVGKQ KDYSEGSDKH NAVSRLVAVS
NLINQAVGDA LSGLLLVEVI LQHMGWSVQK WNELYKDLPS KQVKVEVPDR TAVVTTSEET
EALKPLGIQD AINGEIKKYQ RGRAFIRPSG TEDVVRVYAE ASTQEAADSL ASSVAQLVKS
FLGSS
//
