ID   PGKH_CHLRE              Reviewed;         461 AA.
AC   P41758;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   22-JUL-2008, entry version 44.
DE   RecName: Full=Phosphoglycerate kinase, chloroplastic;
DE            EC=2.7.2.3;
DE   Flags: Precursor;
OS   Chlamydomonas reinhardtii.
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=95241622; PubMed=7724671; DOI=10.1104/pp.107.2.393;
RA   Kitayama M., Togasaki R.K.;
RT   "Purification and cDNA isolation of chloroplastic phosphoglycerate
RT   kinase from Chlamydomonas reinhardtii.";
RL   Plant Physiol. 107:393-400(1995).
CC   -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC       D-glyceroyl phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
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DR   EMBL; U14912; AAA70082.1; -; mRNA.
DR   PIR; T08041; T08041.
DR   HSSP; P18912; 1PHP.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   Gene3D; G3DSA:3.40.50.1270; Phosphoglycerate_kinase_C; 1.
DR   Gene3D; G3DSA:3.40.50.1260; Phosphoglycerate_kinase_N; 1.
DR   PANTHER; PTHR11406; PGK; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calvin cycle; Chloroplast; Direct protein sequencing;
KW   Kinase; Nucleotide-binding; Plastid; Transferase; Transit peptide.
FT   TRANSIT       1     60       Chloroplast (Potential).
FT   CHAIN        61    461       Phosphoglycerate kinase, chloroplastic.
FT                                /FTId=PRO_0000023890.
FT   NP_BIND     417    420       ATP (By similarity).
FT   REGION       83     85       Substrate binding (By similarity).
FT   REGION      123    126       Substrate binding (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     182    182       Substrate (By similarity).
FT   BINDING     215    215       Substrate (By similarity).
FT   BINDING     266    266       ATP (By similarity).
FT   BINDING     357    357       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     388    388       ATP (By similarity).
SQ   SEQUENCE   461 AA;  49008 MW;  BA886FDD9E4DCCB9 CRC64;
     MALSMKMRAN ARVSGRRVAA VAPRVVPFSS ASSSVLRSGF ALRCLWTSAA WAALASVVEA
     VKKSVGDLHK ADLEGKRVFV RADLNVPLDK ATLAITDDTR IRAAVPTLKY LLDNGAKVLL
     TSHLGRPKGG PEDKYRLTPV VARLSELLGK PVTKVDDCIG PEVEKAVGAM KNGELLLLEN
     CRFYKEEEKN EPEFAKKLAA NADLYVNDAF GTAHRAHAST EGVTKFLKPS VAGFLLQKEL
     DYLDGAVSNP KRPFVAIVGG SKVSSKITVI EALMEKCDKI IIGGGMIFTF YKARALKVGS
     SLVEDDKIEL AKKLEEMAKA KGVQLLLPTD VVVADKFDAN ANTQTVPITA IPDGWMGLDI
     GPDSVKTFND ALADAKTVVW NGPMGVFEFP QVRQRTVSIA NTLAGLTPKG CITIIGGGDS
     VAAVEQAGVA EKMSHISTGG GASLELLEGK VLPGVAALDE K
//