PMG1_ARATH
ID PMG1_ARATH Reviewed; 557 AA.
AC O04499; Q8H161; Q8LD62; Q93ZF2; Q94AY0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1;
DE Short=BPG-independent PGAM 1;
DE Short=Phosphoglyceromutase 1;
DE EC=5.4.2.12 {ECO:0000269|PubMed:21813794};
DE AltName: Full=PGAM-I 1;
GN Name=PGM1; OrderedLocusNames=At1g09780 {ECO:0000312|Araport:AT1G09780};
GN ORFNames=F21M12.16 {ECO:0000312|EMBL:AAB60731.1};
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].
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].
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 [5]
RP REVIEW.
RX PubMed=15333754; DOI=10.1104/pp.104.044610;
RA Wang R., Tischner R., Gutierrez R.A., Hoffman M., Xing X., Chen M.,
RA Coruzzi G., Crawford N.M.;
RT "Genomic analysis of the nitrate response using a nitrate reductase-null
RT mutant of Arabidopsis.";
RL Plant Physiol. 136:2512-2522(2004).
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60731.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000132; AAB60731.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28491.1; -; Genomic_DNA.
DR EMBL; AY045627; AAK73985.1; -; mRNA.
DR EMBL; AY057581; AAL09820.1; -; mRNA.
DR EMBL; AY081722; AAL87375.1; -; mRNA.
DR EMBL; AY150432; AAN12974.1; -; mRNA.
DR EMBL; BT000692; AAN31837.1; -; mRNA.
DR EMBL; BT000773; AAN31912.1; -; mRNA.
DR EMBL; AY086182; AAM64261.1; -; mRNA.
DR PIR; G86231; G86231.
DR RefSeq; NP_563852.1; NM_100850.3.
DR AlphaFoldDB; O04499; -.
DR SMR; O04499; -.
DR BioGRID; 22748; 23.
DR STRING; 3702.AT1G09780.1; -.
DR iPTMnet; O04499; -.
DR MetOSite; O04499; -.
DR PaxDb; O04499; -.
DR PRIDE; O04499; -.
DR ProteomicsDB; 234977; -.
DR EnsemblPlants; AT1G09780.1; AT1G09780.1; AT1G09780.
DR GeneID; 837507; -.
DR Gramene; AT1G09780.1; AT1G09780.1; AT1G09780.
DR KEGG; ath:AT1G09780; -.
DR Araport; AT1G09780; -.
DR TAIR; locus:2024357; AT1G09780.
DR eggNOG; KOG4513; Eukaryota.
DR HOGENOM; CLU_026099_3_1_1; -.
DR InParanoid; O04499; -.
DR OMA; NCIHNAP; -.
DR OrthoDB; 304612at2759; -.
DR PhylomeDB; O04499; -.
DR BioCyc; ARA:AT1G09780-MON; -.
DR BRENDA; 5.4.2.12; 399.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:O04499; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04499; baseline and differential.
DR Genevisible; O04499; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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:0009409; P:response to cold; IEP:TAIR.
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 Cytoplasm; Glycolysis; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..557
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase 1"
FT /id="PRO_0000212108"
FT ACT_SITE 80
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 169..170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 285..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 429
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 470
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 500
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT CONFLICT 124
FT /note="T -> A (in Ref. 3; AAN31837)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="R -> G (in Ref. 3; AAL09820)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="F -> I (in Ref. 3; AAN31837)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="T -> K (in Ref. 3; AAK73985/AAL87375)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="P -> L (in Ref. 3; AAN31837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 60580 MW; D5FC3D06A963B9AB CRC64;
MATSSAWKLD DHPKLPKGKT IAVIVLDGWG ESAPDQYNCI HNAPTPAMDS LKHGAPDTWT
LIKAHGTAVG LPSEDDMGNS EVGHNALGAG RIFAQGAKLC DQALASGKIF EGEGFKYVSE
SFETNTLHLV GLLSDGGVHS RLDQLQLLIK GSAERGAKRI RVHILTDGRD VLDGSSVGFV
ETLEADLVAL RENGVDAQIA SGGGRMYVTL DRYENDWEVV KRGWDAQVLG EAPHKFKNAV
EAVKTLRKEP GANDQYLPPF VIVDESGKAV GPIVDGDAVV TFNFRADRMV MHAKALEYED
FDKFDRVRYP KIRYAGMLQY DGELKLPSRY LVSPPEIDRT SGEYLTHNGV STFACSETVK
FGHVTFFWNG NRSGYFNEKL EEYVEIPSDS GISFNVQPKM KALEIGEKAR DAILSGKFDQ
VRVNIPNGDM VGHTGDIEAT VVACEAADLA VKMIFDAIEQ VKGIYVVTAD HGNAEDMVKR
DKSGKPALDK EGKLQILTSH TLKPVPIAIG GPGLAQGVRF RKDLETPGLA NVAATVMNLH
GFVAPSDYEP TLIEVVE
