PLAS_DRYCA
ID PLAS_DRYCA Reviewed; 102 AA.
AC Q7SIB8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Plastocyanin;
GN Name=PETE;
OS Dryopteris crassirhizoma (Thick stemmed wood fern).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae; Dryopteridaceae;
OC Dryopteridoideae; Dryopteris.
OX NCBI_TaxID=97234;
RN [1]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH
RP COPPER, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf;
RX PubMed=10206999; DOI=10.1074/jbc.274.17.11817;
RA Kohzuma T., Inoue T., Yoshizaki F., Sasakawa Y., Onodera K., Nagatomo S.,
RA Kitagawa T., Uzawa S., Isobe Y., Sugimura Y., Gotowda M., Kai Y.;
RT "The structure and unusual pH dependence of plastocyanin from the fern
RT Dryopteris crassirhizoma. The protonation of an active site histidine is
RT hindered by pi-pi interactions.";
RL J. Biol. Chem. 274:11817-11823(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER, FUNCTION,
RP COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=10529231; DOI=10.1021/bi990502t;
RA Inoue T., Gotowda M., Sugawara H., Kohzuma T., Yoshizaki F., Sugimura Y.,
RA Kai Y.;
RT "Structure comparison between oxidized and reduced plastocyanin from a
RT fern, Dryopteris crassirhizoma.";
RL Biochemistry 38:13853-13861(1999).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:10206999,
CC ECO:0000269|PubMed:10529231}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:10206999, ECO:0000269|PubMed:10529231};
CC Note=The crystal structure with reduced Cu(1+) has also been determined
CC (PubMed:10206999, PubMed:10529231).;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10206999, ECO:0000269|PubMed:10529231}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10206999,
CC ECO:0000269|PubMed:10529231}; Lumenal side
CC {ECO:0000269|PubMed:10206999, ECO:0000269|PubMed:10529231}.
CC Note=Loosely bound to the inner thylakoid membrane surface in
CC chloroplasts (PubMed:10206999, PubMed:10529231).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR PDB; 1KDI; X-ray; 1.80 A; A=1-102.
DR PDB; 1KDJ; X-ray; 1.70 A; A=1-102.
DR PDB; 2BZ7; X-ray; 1.76 A; A=1-102.
DR PDB; 2BZC; X-ray; 1.79 A; A=1-102.
DR PDBsum; 1KDI; -.
DR PDBsum; 1KDJ; -.
DR PDBsum; 2BZ7; -.
DR PDBsum; 2BZC; -.
DR AlphaFoldDB; Q7SIB8; -.
DR BMRB; Q7SIB8; -.
DR SMR; Q7SIB8; -.
DR EvolutionaryTrace; Q7SIB8; -.
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 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..102
FT /note="Plastocyanin"
FT /id="PRO_0000085565"
FT DOMAIN 1..102
FT /note="Plastocyanin-like"
FT BINDING 37
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10206999,
FT ECO:0000269|PubMed:10529231"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10206999,
FT ECO:0000269|PubMed:10529231"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10206999,
FT ECO:0000269|PubMed:10529231"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10206999,
FT ECO:0000269|PubMed:10529231"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1KDJ"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:1KDJ"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1KDJ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1KDJ"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:1KDJ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2BZ7"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1KDJ"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1KDJ"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2BZC"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1KDJ"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1KDJ"
SQ SEQUENCE 102 AA; 10776 MW; 8F061F107483C094 CRC64;
AKVEVGDEVG NFKFYPDSIT VSAGEAVEFT LVGETGHNIV FDIPAGAPGT VASELKAASM
DENDLLSEDE PSFKAKVSTP GTYTFYCTPH KSANMKGTLT VK
