AGM1_ARATH
ID AGM1_ARATH Reviewed; 556 AA.
AC P57750; Q05211;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phosphoacetylglucosamine mutase;
DE Short=PAGM;
DE EC=5.4.2.3;
DE AltName: Full=Acetylglucosamine phosphomutase;
DE AltName: Full=DNA-damage-repair/toleration protein DRT101;
DE AltName: Full=N-acetylglucosamine-phosphate mutase;
GN Name=DRT101; OrderedLocusNames=At5g18070; ORFNames=MRG7.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 183-556.
RC STRAIN=cv. Columbia;
RX PubMed=8329681; DOI=10.1007/bf00015972;
RA Pang Q., Hays J.B., Rajagopal I., Schaefer T.S.;
RT "Selection of Arabidopsis cDNAs that partially correct phenotypes of
RT Escherichia coli DNA-damage-sensitive mutants and analysis of two plant
RT cDNAs that appear to express UV-specific dark repair activities.";
RL Plant Mol. Biol. 22:411-426(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA72352.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB012246; BAB09465.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92503.1; -; Genomic_DNA.
DR EMBL; AY075620; AAL91631.1; -; mRNA.
DR EMBL; L11367; AAA72352.1; ALT_SEQ; mRNA.
DR PIR; S35270; S35270.
DR RefSeq; NP_568359.2; NM_121812.3.
DR AlphaFoldDB; P57750; -.
DR SMR; P57750; -.
DR BioGRID; 17202; 1.
DR STRING; 3702.AT5G18070.1; -.
DR iPTMnet; P57750; -.
DR PaxDb; P57750; -.
DR PRIDE; P57750; -.
DR ProteomicsDB; 244657; -.
DR EnsemblPlants; AT5G18070.1; AT5G18070.1; AT5G18070.
DR GeneID; 831926; -.
DR Gramene; AT5G18070.1; AT5G18070.1; AT5G18070.
DR KEGG; ath:AT5G18070; -.
DR Araport; AT5G18070; -.
DR TAIR; locus:2172294; AT5G18070.
DR eggNOG; KOG2537; Eukaryota.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; P57750; -.
DR OMA; WEAYATK; -.
DR OrthoDB; 345441at2759; -.
DR PhylomeDB; P57750; -.
DR BioCyc; ARA:AT5G18070-MON; -.
DR UniPathway; UPA00113; UER00530.
DR PRO; PR:P57750; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P57750; baseline and differential.
DR Genevisible; P57750; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 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.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..556
FT /note="Phosphoacetylglucosamine mutase"
FT /id="PRO_0000148015"
FT ACT_SITE 68
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 386..388
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 518..522
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 556 AA; 60391 MW; BCADE44F14DDC3D0 CRC64;
MDEIQIASIL KSSELFPIPQ GVKLSYGTAG FRGDAKLLES TVYRVGILSA LRSLKLGSAT
VGLMITASHN KVSDNGIKVS DPSGFMLSQE WEPFADQIAN ASSPEELVSL IRKFMEKEEI
AIGENNKGAE VWLGRDTRPS GESLLRAGEI GVGSILGSVA IDIGILTTPQ LHWMVRAKNK
GLKATENDYF ENLSTSFRCL IDLIPSSGND KLEISKLLVD GANGVGGQKI EKLRGSLSNL
DVEIRNTGRD GGVLNEGVGA DFVQKEKVLP VGFGFKDVGM RCASLDGDAD RLVYFYIPSD
SSEKVELLDG DKILSLFALF IKEQLNALED DEERKQSRLG VVQTAYANGA STDYLKHLGL
DVVFAKTGVK HLHEKAAEFD IGIYFEANGH GTILFSESFL SWLVSKQKDL TAKGQGGSEE
HKAVSRLMAV SNLINQAVGD ALSGVLLVEV ILQHLGWSIE KWNELYKDLP SRQIKVEVPD
RTAVVTTSEE TEALRPMGIQ DAINSEIKKY SRGRAFIRPS GTEDVVRVYA EASTQEDADS
LANSVAQLVK SFLGSS
