PGKH1_ARATH
ID PGKH1_ARATH Reviewed; 481 AA.
AC Q9LD57;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphoglycerate kinase 1, chloroplastic {ECO:0000303|Ref.1};
DE EC=2.7.2.3 {ECO:0000250|UniProtKB:P00558};
DE Flags: Precursor;
GN Name=PGK1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At3g12780 {ECO:0000312|Araport:AT3G12780};
GN ORFNames=MBK21.15 {ECO:0000312|EMBL:BAB02423.1};
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 [MRNA].
RA Shih M.-C.;
RT "Structure and regulation of nuclear genes encoding chloroplast and
RT cytosolic phosphoglycerate kinase in Arabidopsis thaliana.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-481.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=10520454; DOI=10.3109/10425179809008459;
RA Loebler M.;
RT "Two phosphoglycerate kinase cDNAs from Arabidopsis thaliana.";
RL DNA Seq. 8:247-252(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH FTSZ2-1 AND FTSZ2-2.
RX PubMed=22823492; DOI=10.1042/bj20120404;
RA Gargano D., Maple-Groedem J., Moeller S.G.;
RT "In vivo phosphorylation of FtsZ2 in Arabidopsis thaliana.";
RL Biochem. J. 446:517-521(2012).
CC -!- FUNCTION: May trigger the phosphorylation of FTSZ2-1 and FTSZ2-2.
CC {ECO:0000269|PubMed:22823492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000250|UniProtKB:P00558};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle. {ECO:0000305}.
CC -!- SUBUNIT: Monomer (By similarity). Binds to FTSZ2-1 and FTSZ2-2
CC (PubMed:22823492). {ECO:0000250|UniProtKB:P00558,
CC ECO:0000269|PubMed:22823492}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; AF247558; AAF70258.1; -; mRNA.
DR EMBL; AB024033; BAB02423.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75246.1; -; Genomic_DNA.
DR EMBL; AF360234; AAK25944.1; -; mRNA.
DR EMBL; AF428418; AAL16186.1; -; mRNA.
DR EMBL; AY045623; AAK73981.1; -; mRNA.
DR EMBL; AY059841; AAL24323.1; -; mRNA.
DR EMBL; AY062953; AAL33785.1; -; mRNA.
DR EMBL; AY093998; AAM16259.1; -; mRNA.
DR EMBL; AY114638; AAM47957.1; -; mRNA.
DR EMBL; AY126991; AAM83218.1; -; mRNA.
DR EMBL; AK227225; BAE99262.1; -; mRNA.
DR EMBL; AK316922; BAH19627.1; -; mRNA.
DR EMBL; U37701; AAB60303.1; -; mRNA.
DR PIR; S71368; S71368.
DR RefSeq; NP_187884.1; NM_112114.4.
DR AlphaFoldDB; Q9LD57; -.
DR SMR; Q9LD57; -.
DR BioGRID; 5795; 11.
DR IntAct; Q9LD57; 1.
DR MINT; Q9LD57; -.
DR STRING; 3702.AT3G12780.1; -.
DR iPTMnet; Q9LD57; -.
DR MetOSite; Q9LD57; -.
DR World-2DPAGE; 0003:Q9LD57; -.
DR PaxDb; Q9LD57; -.
DR PRIDE; Q9LD57; -.
DR ProteomicsDB; 235116; -.
DR EnsemblPlants; AT3G12780.1; AT3G12780.1; AT3G12780.
DR GeneID; 820461; -.
DR Gramene; AT3G12780.1; AT3G12780.1; AT3G12780.
DR KEGG; ath:AT3G12780; -.
DR Araport; AT3G12780; -.
DR TAIR; locus:2087750; AT3G12780.
DR eggNOG; KOG1367; Eukaryota.
DR HOGENOM; CLU_025427_0_2_1; -.
DR InParanoid; Q9LD57; -.
DR OMA; GMNIANS; -.
DR OrthoDB; 838642at2759; -.
DR PhylomeDB; Q9LD57; -.
DR BioCyc; ARA:AT3G12780-MON; -.
DR BRENDA; 2.7.2.3; 399.
DR UniPathway; UPA00116; -.
DR PRO; PR:Q9LD57; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LD57; baseline and differential.
DR Genevisible; Q9LD57; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IGI:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IGI:TAIR.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calvin cycle; Chloroplast; Kinase; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..481
FT /note="Phosphoglycerate kinase 1, chloroplastic"
FT /id="PRO_0000407930"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 139..142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT BINDING 432..435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 481 AA; 50112 MW; F27EE9BF7F2062EF CRC64;
MASAAASSAF SLLKSTGAVA SSAGTRARAS LLPIPSTSVS ARPLGFSATL DSRRFSLHVA
SKVESVRGKG SRGVVSMAKK SVGDLTSADL KGKKVFVRAD LNVPLDDNQT ITDDTRIRAA
IPTIKYLIEN GAKVILSTHL GRPKGVTPKF SLAPLVPRLS ELLGIEVTKA DDCIGPEVES
LVASLPEGGV LLLENVRFYK EEEKNDPEFA KKLASLADLY VNDAFGTAHR AHASTEGVTK
FLKPSVAGFL LQKELDYLVG AVSNPKRPFA AIVGGSKVSS KIGVIESLLE KCDILLLGGG
MIFTFYKAQG LSVGSSLVEE DKLELATELL AKAKAKGVSL LLPTDVVVAD KFAPDANSKI
VPASGIEDGW MGLDIGPDSI KTFNEALDTT QTVIWNGPMG VFEMEKFAAG TEAIANKLAE
LSEKGVTTII GGGDSVAAVE KVGVAGVMSH ISTGGGASLE LLEGKVLPGV IALDEAIPVT
V
