ID A0A1S4BC37_TOBAC Unreviewed; 558 AA.
AC A0A1S4BC37;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=LOC107806772 {ECO:0000313|RefSeq:XP_016486490.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016486490.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016486490.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_016486490.1; XM_016631004.1.
DR AlphaFoldDB; A0A1S4BC37; -.
DR SMR; A0A1S4BC37; -.
DR STRING; 4097.A0A1S4BC37; -.
DR PaxDb; 4097-A0A1S4BC37; -.
DR GeneID; 107806772; -.
DR KEGG; nta:107806772; -.
DR OMA; VLDDGCC; -.
DR OrthoDB; 1475at2759; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000084051; Unplaced.
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; IPR049022; AMG1_III.
DR InterPro; IPR016657; PAGM.
DR PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 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.
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:UP000084051}.
FT DOMAIN 57..89
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 124..177
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 305..457
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 475..549
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 67
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 387..389
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 518..522
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ SEQUENCE 558 AA; 60237 MW; 04C4706F318E5F74 CRC64;
MNEKQQSLLL ESAARFPPPK GVKLSYGTAG FRADASLLES TVFRVGILAA LRSLKTGSVI
GLMITASHNK VADNGIKVAD PSGGMLTQDW EPFSDAIANA PDPHSLLQLI TEFVKKEEIG
FEGRQLAEVL LGRDTRPSGE ALLEAAKQGI TSIIGAIGTD MGVVTTPQLH WMVRARNRGL
EASESCYFHQ LSTSFRCLMD LKPEEISKNG NDATLVVDGA DGVGGEKLEQ FKKMLTGLCI
EVRNRGDGIL NEGVGADYVQ KEKVAPRSFG SADAGLRCAS LDGDADRLVY FSVLSKKNNN
IELVDGDKIL SLFALFIKEQ LSILNEGEGK KGNDSYQARL GVVQTAYANG ASTDYLNEMG
LEVVLTPTGV KYLHEKAAEF DIGIYFEANG HGTILFSEAF LCWLETSHKT LLSTSEGSAK
QKAASRLLAV SQLINQAVGD ALSGLLLVEV ILKYMGWSIH RWNELYHDLP SRQLKVKVVD
RTAVLTANAE TVAVQPIGIQ EAINAEIAKY PRGRCFIRPS GTEDVIRVYA EATSQDAADA
LASSVAKLVD QYLGFGSS
//