GenomeNet

Database: UniProt
Entry: A0A1S4BC37_TOBAC
LinkDB: A0A1S4BC37_TOBAC
Original site: A0A1S4BC37_TOBAC 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system