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PGML2_ARATH
ID   PGML2_ARATH             Reviewed;         343 AA.
AC   F4IBB2; F4IBB1; Q0WU57; Q9LQB8; Q9SLV2;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Phosphoglycerate mutase-like protein 2 {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g58280 {ECO:0000312|Araport:AT1G58280};
GN   ORFNames=F19C14.10 {ECO:0000312|EMBL:AAF82259.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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] OF 6-343 (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 20-343 (ISOFORM 2).
RX   PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA   Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT   "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT   genomic region located around the 100 map unit of chromosome 1.";
RL   Gene 239:309-316(1999).
CC   -!- FUNCTION: May play a role in carbohydrates metabolism.
CC       {ECO:0000250|UniProtKB:Q9MAA2}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4IBB2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4IBB2-2; Sequence=VSP_056878;
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF82259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC008051; AAF82259.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE33528.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33529.1; -; Genomic_DNA.
DR   EMBL; AK227327; BAE99341.1; -; mRNA.
DR   EMBL; AB028195; BAA87937.1; -; mRNA.
DR   PIR; D96616; D96616.
DR   PIR; T52444; T52444.
DR   RefSeq; NP_176124.2; NM_104608.4. [F4IBB2-2]
DR   RefSeq; NP_849826.2; NM_179495.3. [F4IBB2-1]
DR   AlphaFoldDB; F4IBB2; -.
DR   STRING; 3702.AT1G58280.2; -.
DR   iPTMnet; F4IBB2; -.
DR   PaxDb; F4IBB2; -.
DR   PRIDE; F4IBB2; -.
DR   ProteomicsDB; 235074; -. [F4IBB2-1]
DR   DNASU; 842197; -.
DR   EnsemblPlants; AT1G58280.1; AT1G58280.1; AT1G58280. [F4IBB2-2]
DR   EnsemblPlants; AT1G58280.2; AT1G58280.2; AT1G58280. [F4IBB2-1]
DR   GeneID; 842197; -.
DR   Gramene; AT1G58280.1; AT1G58280.1; AT1G58280. [F4IBB2-2]
DR   Gramene; AT1G58280.2; AT1G58280.2; AT1G58280. [F4IBB2-1]
DR   KEGG; ath:AT1G58280; -.
DR   Araport; AT1G58280; -.
DR   TAIR; locus:2016640; AT1G58280.
DR   eggNOG; KOG4754; Eukaryota.
DR   InParanoid; F4IBB2; -.
DR   OrthoDB; 1063916at2759; -.
DR   PhylomeDB; F4IBB2; -.
DR   PRO; PR:F4IBB2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4IBB2; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
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; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..343
FT                   /note="Phosphoglycerate mutase-like protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000430633"
FT   REGION          322..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        65
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        177
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   SITE            273
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   VAR_SEQ         180..204
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_056878"
FT   CONFLICT        33
FT                   /note="R -> H (in Ref. 3; BAE99341)"
SQ   SEQUENCE   343 AA;  38605 MW;  FAFADCA87B3D988B CRC64;
     MIHQSMTSNL SFYISSVSHL SSPLPSLSRL SLRCCSSLPA HDMETKPSQG LYPLHRCKTI
     HLVRHAQGIH NVEGEKNHKA YLSEDLFDAH LTPLGWQQVD NLHKHVNASG ISNRIELVVV
     SPLLRTLQTA VGTFGGEGYK DGVNTPLLMT AGAGNSDRPA ISRLNRPPFI AVESCREHLV
     CLLFYLLHDW HFLEMKTFAM FLVQGVHPCD RRSNITKYRE LFPAIDFSLI ETDEDVLWKP
     DIREEDKDIA TRGVKFFNWL STRKEKEIAV VTHSGFLYQT LNSFGNDCDP SVKNEISKKF
     VNCELRSFVL VDKCMSSSDP PMTNYPGTIL TGEDASSDIA DQK
 
 
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