PGKH2_ARATH
ID PGKH2_ARATH Reviewed; 478 AA.
AC P50318; Q42542; Q9C7J4; Q9SGU6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphoglycerate kinase 2, chloroplastic;
DE EC=2.7.2.3;
DE Flags: Precursor;
GN OrderedLocusNames=At1g56190; ORFNames=F14G9.19, T6H22.1;
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 [MRNA] OF 248-478.
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 [5]
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).
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 -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P50318-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; AC009894; AAF02830.1; -; Genomic_DNA.
DR EMBL; AC069159; AAG50920.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33356.1; -; Genomic_DNA.
DR EMBL; AY056291; AAL07140.1; -; mRNA.
DR EMBL; AY099598; AAM20449.1; -; mRNA.
DR EMBL; BT000250; AAN15569.1; -; mRNA.
DR EMBL; U37700; AAA79705.1; -; mRNA.
DR PIR; D96603; D96603.
DR PIR; S71214; S71214.
DR RefSeq; NP_176015.1; NM_104498.4. [P50318-1]
DR AlphaFoldDB; P50318; -.
DR SMR; P50318; -.
DR BioGRID; 27297; 7.
DR STRING; 3702.AT1G56190.1; -.
DR iPTMnet; P50318; -.
DR PaxDb; P50318; -.
DR PRIDE; P50318; -.
DR ProteomicsDB; 234996; -. [P50318-1]
DR EnsemblPlants; AT1G56190.1; AT1G56190.1; AT1G56190. [P50318-1]
DR GeneID; 842072; -.
DR Gramene; AT1G56190.1; AT1G56190.1; AT1G56190. [P50318-1]
DR KEGG; ath:AT1G56190; -.
DR Araport; AT1G56190; -.
DR TAIR; locus:2205215; AT1G56190.
DR eggNOG; KOG1367; Eukaryota.
DR InParanoid; P50318; -.
DR BioCyc; ARA:AT1G56190-MON; -.
DR BRENDA; 2.7.2.3; 399.
DR UniPathway; UPA00116; -.
DR PRO; PR:P50318; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P50318; baseline and differential.
DR Genevisible; P50318; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
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; IMP:TAIR.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IMP: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 Alternative splicing; ATP-binding; Calvin cycle; Chloroplast; Kinase;
KW Nucleotide-binding; Phosphoprotein; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 75..478
FT /note="Phosphoglycerate kinase 2, chloroplastic"
FT /id="PRO_0000023889"
FT BINDING 97..99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136..139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 429..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LD57"
FT CONFLICT 412
FT /note="A -> R (in Ref. 4; AAA79705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 49939 MW; 03751560F052E6F8 CRC64;
MASTAATAAL SIIKSTGGAA VTRSSRASFG HIPSTSVSAR RLGFSAVVDS RFSVHVASKV
HSVRGKGARG VITMAKKSVG DLNSVDLKGK KVFVRADLNV PLDDNQNITD DTRIRAAIPT
IKFLIENGAK VILSTHLGRP KGVTPKFSLA PLVPRLSELL GIEVVKADDC IGPEVETLVA
SLPEGGVLLL ENVRFYKEEE KNEPDFAKKL ASLADLYVND AFGTAHRAHA STEGVTKFLK
PSVAGFLLQK ELDYLVGAVS NPKRPFAAIV GGSKVSSKIG VIESLLEKCD ILLLGGGMIF
TFYKAQGLSV GSSLVEEDKL ELATTLLAKA KARGVSLLLP TDVVIADKFA PDANSKIVPA
SAIPDGWMGL DIGPDSVKTF NEALDTTQTV IWNGPMGVFE FEKFAKGTEA VANKLAELSK
KGVTTIIGGG DSVAAVEKVG VAGVMSHIST GGGASLELLE GKVLPGVVAL DEATPVTV
