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   24-JAN-2024, entry version 151.
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.P50318; -.
DR   iPTMnet; P50318; -.
DR   PaxDb; 3702-AT1G56190-1; -.
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; AT1G56190; CPGK2.
DR   eggNOG; KOG1367; Eukaryota.
DR   InParanoid; P50318; -.
DR   OrthoDB; 5477183at2759; -.
DR   BioCyc; ARA:AT1G56190-MONOMER; -.
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   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR   GO; GO:0019375; P:galactolipid biosynthetic process; IGI:TAIR.
DR   GO; GO:0006096; P:glycolytic process; IMP:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR   Genevisible; P50318; AT.
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
//