AGM1_ORYSJ
ID AGM1_ORYSJ Reviewed; 562 AA.
AC Q6ZDQ1; A0A0N7KN29; Q0D7Z2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphoacetylglucosamine mutase;
DE Short=PAGM;
DE EC=5.4.2.3;
DE AltName: Full=Acetylglucosamine phosphomutase;
DE AltName: Full=N-acetylglucosamine-phosphate mutase;
GN OrderedLocusNames=Os07g0195400 {ECO:0000312|EMBL:BAF21031.1},
GN LOC_Os07g09720 {ECO:0000305};
GN ORFNames=OJ1715_A07.21, OsJ_23435 {ECO:0000312|EMBL:EEE66741.1},
GN P0589E08.4;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Interconverts GlcNAc-6-P and GlcNAc-1-P. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9P4V2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2};
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 -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AP003848; BAD30377.1; -; Genomic_DNA.
DR EMBL; AP004379; BAC83577.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21031.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00466.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE66741.1; -; Genomic_DNA.
DR EMBL; AK069901; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015644787.1; XM_015789301.1.
DR AlphaFoldDB; Q6ZDQ1; -.
DR SMR; Q6ZDQ1; -.
DR STRING; 4530.OS07T0195400-01; -.
DR PaxDb; Q6ZDQ1; -.
DR PRIDE; Q6ZDQ1; -.
DR EnsemblPlants; Os07t0195400-01; Os07t0195400-01; Os07g0195400.
DR GeneID; 4342646; -.
DR Gramene; Os07t0195400-01; Os07t0195400-01; Os07g0195400.
DR KEGG; osa:4342646; -.
DR eggNOG; KOG2537; Eukaryota.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; Q6ZDQ1; -.
DR OMA; WEAYATK; -.
DR OrthoDB; 345441at2759; -.
DR PlantReactome; R-OSA-1119386; UDP-N-acetylgalactosamine biosynthesis.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q6ZDQ1; OS.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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 InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-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; IPR016657; PAGM.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PIRSF; PIRSF016408; PAGM; 1.
DR SUPFAM; SSF53738; SSF53738; 4.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..562
FT /note="Phosphoacetylglucosamine mutase"
FT /id="PRO_0000247307"
FT ACT_SITE 74
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 395..397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 526..530
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT CONFLICT 211
FT /note="K -> E (in Ref. 5; AK069901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 60344 MW; CC80059ED8ECBC0D CRC64;
MAELAAGGDQ RAALLAAATL FPPPPDGARF SYGTAGFRAE GAAMGPAVCR AGVVAALRSA
KLGGAAVGVV ITASHNPVRD NGVKIVDADG GMLSQDWEPF ADALANAPNP DALLQIVLQF
AKDEDIKLGG SHSAQVLLAR DTRPTGEYLL DVAVKGVNAV IGAVAVDMGI LTTPQLHWMV
RSKNKGLKSS ETDYFSQVID SFRCLLELVP KDKEADVINN RLIVDGANGI GGLKLEEIKA
KISGLDIHVR NSGKGEGILN ESCGADFVQK EKVVPLGFGP EDVGFRCASF DGDADRLVYF
RIVSSSDTRI DLVDGDKILS LFVLFIREQL DIINGKDNKG NEVLPTRFGV IQTAYANGAS
TDFLKNIGLE VVFTPTGVKY LHKEALKYDI GIYFEANGHG TVLFSDHFVS QLESLTSEFS
SKAAGSSQHQ AAMRLLATSQ LINQAVGDAL SGMLLVEAVL QYKGWSFQNW CDLYTDLPSR
QLKVKVQDRN SIVTTDAERR VCQPNGLQEL IDGEISNYSH GRCFVRPSGT EDVVRVYAEA
SSEEAADCLA KRVAQHVERI LG
