PMG2_ARATH
ID PMG2_ARATH Reviewed; 560 AA.
AC Q9M9K1; A0A178VFA2; B9DFU6; Q8LF55;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2;
DE Short=BPG-independent PGAM 2;
DE Short=Phosphoglyceromutase 2;
DE EC=5.4.2.12 {ECO:0000269|PubMed:21813794};
DE AltName: Full=PGAM-I 2;
GN Name=PGM2; OrderedLocusNames=At3g08590 {ECO:0000312|Araport:AT3G08590};
GN ORFNames=F17O14.6 {ECO:0000312|EMBL:AAG51361.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=21813794; DOI=10.1093/jxb/err223;
RA Zhao Z., Assmann S.M.;
RT "The glycolytic enzyme, phosphoglycerate mutase, has critical roles in
RT stomatal movement, vegetative growth, and pollen production in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 62:5179-5189(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA)
CC and 3-phosphoglycerate (3-PGA) (PubMed:21813794). Required for guard
CC cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-
CC regulated stomatal movements) and fertility (e.g. pollen grains
CC production) (PubMed:21813794). {ECO:0000269|PubMed:21813794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000269|PubMed:21813794};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9X519};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9X519};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000250|UniProtKB:Q9X519}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9X519}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21813794). Plants
CC missing both PGM1 and PGM2 have no detectable phosphoglycerate mutase
CC activity and show defects in blue light-, abscisic acid- (ABA), and low
CC CO(2)-regulated stomatal movements (PubMed:21813794). The double mutant
CC ipgam1 ipgam2 exhibits a severely impaired vegetative growth with pale
CC reticulate leaves and don't produce pollen (PubMed:21813794).
CC {ECO:0000269|PubMed:21813794}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; AC012562; AAG51361.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74650.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74651.1; -; Genomic_DNA.
DR EMBL; AY039969; AAK64146.1; -; mRNA.
DR EMBL; AF424615; AAL11608.1; -; mRNA.
DR EMBL; AY113910; AAM44958.1; -; mRNA.
DR EMBL; AK316907; BAH19613.1; -; mRNA.
DR EMBL; AY085044; AAM61601.1; -; mRNA.
DR RefSeq; NP_187471.1; NM_111693.3.
DR RefSeq; NP_850542.1; NM_180211.2.
DR AlphaFoldDB; Q9M9K1; -.
DR SMR; Q9M9K1; -.
DR BioGRID; 5341; 25.
DR STRING; 3702.AT3G08590.2; -.
DR iPTMnet; Q9M9K1; -.
DR PaxDb; Q9M9K1; -.
DR PRIDE; Q9M9K1; -.
DR ProteomicsDB; 234979; -.
DR EnsemblPlants; AT3G08590.1; AT3G08590.1; AT3G08590.
DR EnsemblPlants; AT3G08590.2; AT3G08590.2; AT3G08590.
DR GeneID; 820006; -.
DR Gramene; AT3G08590.1; AT3G08590.1; AT3G08590.
DR Gramene; AT3G08590.2; AT3G08590.2; AT3G08590.
DR KEGG; ath:AT3G08590; -.
DR Araport; AT3G08590; -.
DR TAIR; locus:2077793; AT3G08590.
DR eggNOG; KOG4513; Eukaryota.
DR HOGENOM; CLU_026099_3_1_1; -.
DR InParanoid; Q9M9K1; -.
DR OMA; FMDGRDT; -.
DR OrthoDB; 304612at2759; -.
DR PhylomeDB; Q9M9K1; -.
DR BioCyc; ARA:AT3G08590-MON; -.
DR BRENDA; 5.4.2.12; 399.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:Q9M9K1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9K1; baseline and differential.
DR Genevisible; Q9M9K1; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IGI:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009555; P:pollen development; IGI:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IGI:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IGI:UniProtKB.
DR GO; GO:0010037; P:response to carbon dioxide; IGI:UniProtKB.
DR GO; GO:0010118; P:stomatal movement; IGI:UniProtKB.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Glycolysis; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..560
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase 2"
FT /id="PRO_0000212109"
FT ACT_SITE 82
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 29
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 171..172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 287..290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 431
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 435
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 502
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 194
FT /note="A -> S (in Ref. 5; AAM61601)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="S -> P (in Ref. 5; AAM61601)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="N -> S (in Ref. 5; AAM61601)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="R -> L (in Ref. 5; AAM61601)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="R -> H (in Ref. 5; AAM61601)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="D -> N (in Ref. 5; AAM61601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 60764 MW; 4D5AC08074D7BB8B CRC64;
MGSSGDVNWK LADHPKLPKG KTIGLIVLDG WGESDPDQYN CIHKAPTPAM DSLKDGKPDT
WRLIKAHGTA VGLPSEDDMG NSEVGHNALG AGRIYAQGAK LVDLALASGK IYEDEGFKYI
SQSFEKGTVH LIGLLSDGGV HSRLDQVQLL LKGFAERGAK RIRVHILTDG RDVLDGSSVG
FVETLEADLA ALRAKGVDAQ VASGGGRMYV TMDRYENDWS VVKRGWDAQV LGEAPHKFKS
ALEAVKTLRA EPGANDQYLP SFVIVDDNGK AVGPIVDGDA VVTFNFRADR MVMHAKALEY
KDFDKFDRVR VPDIRYAGML QYDGELKLPS RYLVSPPLID RTSGEYLAHN GVRTFACSET
VKFGHVTFFW NGNRSGYFNE KLEEYVEIPS DSGISFNVQP KMKALEIAEK ARDAILSGKF
DQVRVNLPNG DMVGHTGDIE ATVVACEAAD RAVRTILDAI EQVGGIYVVT ADHGNAEDMV
KRDKSGKPAL DKEGNLQILT SHTLKPVPIA IGGPGLSAGV RFRQDIETPG LANVAATVMN
LHGFVAPSDY ETSLIEVVEK
