ID   PLAS_ANAVA              Reviewed;         105 AA.
AC   P0C178; P00301; P14114;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Plastocyanin;
GN   Name=petE;
OS   Anabaena variabilis.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=264691;
RN   [1]
RP   STRUCTURE BY NMR IN COMPLEX WITH COPPER, COFACTOR, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=PCC 7118 / ATCC 27892;
RX   PubMed=8679527; DOI=10.1021/bi960621y;
RA   Badsberg U., Joergensen A.M., Gesmar H., Led J.L., Hammerstad J.M.,
RA   Jespersoen L.-L., Ulstrup J.;
RT   "Solution structure of reduced plastocyanin from the blue-green alga
RT   Anabaena variabilis.";
RL   Biochemistry 35:7021-7031(1996).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I. {ECO:0000255|HAMAP-
CC       Rule:MF_00566}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:8679527};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000269|PubMed:8679527}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:8679527}; Lumenal side
CC       {ECO:0000269|PubMed:8679527}. Note=Loosely bound to the thylakoid inner
CC       membrane surface (PubMed:8679527).
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00566}.
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DR   PDB; 1NIN; NMR; -; A=1-105.
DR   PDB; 2GIM; X-ray; 1.60 A; A/C=1-105.
DR   PDBsum; 1NIN; -.
DR   PDBsum; 2GIM; -.
DR   AlphaFoldDB; P0C178; -.
DR   BMRB; P0C178; -.
DR   SMR; P0C178; -.
DR   EvolutionaryTrace; P0C178; -.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04219; Plastocyanin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   HAMAP; MF_00566; Cytb6_f_plastocyanin; 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   InterPro; IPR023511; Plastocyanin_cyanobac.
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; Copper; Electron transport; Membrane; Metal-binding;
KW   Thylakoid; Transport.
FT   CHAIN           1..105
FT                   /note="Plastocyanin"
FT                   /id="PRO_0000228715"
FT   DOMAIN          1..105
FT                   /note="Plastocyanin-like"
FT   BINDING         39
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:8679527,
FT                   ECO:0007744|PDB:1NIN"
FT   BINDING         89
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:8679527,
FT                   ECO:0007744|PDB:1NIN"
FT   BINDING         92
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:8679527,
FT                   ECO:0007744|PDB:1NIN"
FT   BINDING         97
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:8679527,
FT                   ECO:0007744|PDB:1NIN"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:1NIN"
FT   STRAND          14..23
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   HELIX           53..59
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:2GIM"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:2GIM"
SQ   SEQUENCE   105 AA;  11104 MW;  5E540C2E16366DDC CRC64;
     ETYTVKLGSD KGLLVFEPAK LTIKPGDTVE FLNNKVPPHN VVFDAALNPA KSADLAKSLS
     HKQLLMSPGQ STSTTFPADA PAGEYTFYCE PHRGAGMVGK ITVAG