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PGM_ARATH
ID   PGM_ARATH               Reviewed;         271 AA.
AC   Q8GY96;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Phosphoglycerate mutase-like protein {ECO:0000303|PubMed:15010616};
DE            Short=AtPGM {ECO:0000303|PubMed:15010616};
GN   Name=PGM {ECO:0000303|PubMed:15010616};
GN   OrderedLocusNames=At2g17280 {ECO:0000312|Araport:AT2G17280}; ORFNames=F5J6;
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 {ECO:0000312|EMBL:BAC42426.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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   [5]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15010616; DOI=10.1023/b:plan.0000019062.80459.80;
RA   Mazarei M., Lennon K.A., Puthoff D.P., Rodermel S.R., Baum T.J.;
RT   "Expression of an Arabidopsis phosphoglycerate mutase homologue is
RT   localized to apical meristems, regulated by hormones, and induced by
RT   sedentary plant-parasitic nematodes.";
RL   Plant Mol. Biol. 53:513-530(2003).
CC   -!- FUNCTION: May play a role in carbohydrates metabolism.
CC       {ECO:0000250|UniProtKB:Q9MAA2}.
CC   -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem and
CC       meristematic zone of the root tips. {ECO:0000269|PubMed:15010616}.
CC   -!- INDUCTION: By auxin, sucrose, oryzalin and the nematodes Heterodera
CC       schachtii and Meloidogyne incognita in roots. Down-regulated by
CC       abscisic acid (ABA) and hydroxyurea. {ECO:0000269|PubMed:15010616}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; CP002685; AEC06607.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06608.1; -; Genomic_DNA.
DR   EMBL; AK117779; BAC42426.1; -; mRNA.
DR   EMBL; BT006234; AAP12883.1; -; mRNA.
DR   PIR; C84550; C84550.
DR   RefSeq; NP_001077906.1; NM_001084437.2.
DR   RefSeq; NP_179320.1; NM_127283.6.
DR   AlphaFoldDB; Q8GY96; -.
DR   SMR; Q8GY96; -.
DR   STRING; 3702.AT2G17280.2; -.
DR   iPTMnet; Q8GY96; -.
DR   PaxDb; Q8GY96; -.
DR   PRIDE; Q8GY96; -.
DR   ProteomicsDB; 234902; -.
DR   EnsemblPlants; AT2G17280.1; AT2G17280.1; AT2G17280.
DR   EnsemblPlants; AT2G17280.2; AT2G17280.2; AT2G17280.
DR   GeneID; 816234; -.
DR   Gramene; AT2G17280.1; AT2G17280.1; AT2G17280.
DR   Gramene; AT2G17280.2; AT2G17280.2; AT2G17280.
DR   KEGG; ath:AT2G17280; -.
DR   Araport; AT2G17280; -.
DR   TAIR; locus:2827577; AT2G17280.
DR   eggNOG; KOG4754; Eukaryota.
DR   HOGENOM; CLU_039184_4_0_1; -.
DR   InParanoid; Q8GY96; -.
DR   OMA; GRWEDEF; -.
DR   OrthoDB; 1063916at2759; -.
DR   PhylomeDB; Q8GY96; -.
DR   PRO; PR:Q8GY96; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8GY96; baseline and differential.
DR   Genevisible; Q8GY96; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..271
FT                   /note="Phosphoglycerate mutase-like protein"
FT                   /id="PRO_0000430631"
FT   REGION          252..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        22
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        134
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   SITE            205
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
SQ   SEQUENCE   271 AA;  29890 MW;  588088C486752F23 CRC64;
     MDNEGIGLYP LHRCKTIHLV RHAQGIHNVA GEKDHSAYSS EDYFDAHLTP LGWQQVDNLR
     NHVRAAQLLN KVELVIVSPM LRTIQTAVGA FGGEEDTNGA DATPLMVANA GSSDRPAISS
     LNSPPFLAVE LCRETMGDHP CDRRRSVTEY KALFPAIDFS IIETDNDVLW KPSPRESLEE
     VAARGVEFIK WIWTRKEKEI AIVSHSGFLH GLLSSFGKDC CDDLKKELSI HLSNCELRSM
     VIVDRGNLGT DSAETTNYPG KVPEGLDNPS G
 
 
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