PLAS_PHAVU
ID PLAS_PHAVU Reviewed; 99 AA.
AC P00287;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Plastocyanin;
GN Name=PETE;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4462751; DOI=10.1042/bj1430691;
RA Milne P.R., Wells J.R.E., Ambler R.P.;
RT "The amino acid sequence of plastocyanin from French bean (Phaseolus
RT vulgaris).";
RL Biochem. J. 143:691-701(1974).
RN [2]
RP STRUCTURE BY NMR IN COMPLEX WITH COPPER, FUNCTION, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RX PubMed=3172230; DOI=10.1016/0022-2836(88)90291-4;
RA Chazin W.J., Wright P.E.;
RT "Complete assignment of the 1H nuclear magnetic resonance spectrum of
RT French bean plastocyanin. Sequential resonance assignments, secondary
RT structure and global fold.";
RL J. Mol. Biol. 202:623-636(1988).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=1920431; DOI=10.1016/0022-2836(91)80071-2;
RA Moore J.M., Lepre C.A., Gippert G.P., Chazin W.J., Case D.A., Wright P.E.;
RT "High-resolution solution structure of reduced French bean plastocyanin and
RT comparison with the crystal structure of poplar plastocyanin.";
RL J. Mol. Biol. 221:533-555(1991).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:1920431}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:1920431};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:1920431}; Peripheral membrane protein
CC {ECO:0000269|PubMed:1920431}; Lumenal side
CC {ECO:0000269|PubMed:1920431}. Note=Loosely bound to the inner thylakoid
CC membrane surface in chloroplasts (PubMed:1920431).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR PIR; A00297; CUFB.
DR PDB; 9PCY; NMR; -; A=1-99.
DR PDBsum; 9PCY; -.
DR AlphaFoldDB; P00287; -.
DR BMRB; P00287; -.
DR SMR; P00287; -.
DR STRING; 3885.XP_007136129.1; -.
DR PRIDE; P00287; -.
DR EnsemblPlants; ESW08123; ESW08123; PHAVU_009G020300g.
DR Gramene; ESW08123; ESW08123; PHAVU_009G020300g.
DR eggNOG; ENOG502RXIY; Eukaryota.
DR EvolutionaryTrace; P00287; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd04219; Plastocyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR001235; Copper_blue_Plastocyanin.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR002387; Plastocyanin.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00156; COPPERBLUE.
DR PRINTS; PR00157; PLASTOCYANIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR02656; cyanin_plasto; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Copper; Direct protein sequencing;
KW Electron transport; Membrane; Metal-binding; Plastid; Thylakoid; Transport.
FT CHAIN 1..99
FT /note="Plastocyanin"
FT /id="PRO_0000085571"
FT DOMAIN 1..99
FT /note="Plastocyanin-like"
FT BINDING 37
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1920431"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1920431"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1920431"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1920431"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:9PCY"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:9PCY"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:9PCY"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:9PCY"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:9PCY"
SQ SEQUENCE 99 AA; 10492 MW; D529B771D87BDBB9 CRC64;
LEVLLGSGDG SLVFVPSEFS VPSGEKIVFK NNAGFPHNVV FDEDEIPAGV DAVKISMPEE
ELLNAPGETY VVTLDTKGTY SFYCSPHQGA GMVGKVTVN
