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PLAS_PETCR
ID   PLAS_PETCR              Reviewed;          97 AA.
AC   P17341;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Plastocyanin A/B;
GN   Name=PETE;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Festival; TISSUE=Leaf;
RX   PubMed=2365050; DOI=10.1016/0014-5793(90)80904-w;
RA   Dimitrov M.I., Donchev A.A., Egorov C.A.;
RT   "Microheterogeneity of parsley plastocyanin.";
RL   FEBS Lett. 265:141-145(1990).
RN   [2]
RP   PROTEIN SEQUENCE.
RA   Sykes A.G.;
RT   "Structure and electron-transfer reactivity of the blue copper protein
RT   plastocyanin.";
RL   Chem. Soc. Rev. 14:283-315(1985).
RN   [3]
RP   STRUCTURE BY NMR IN COMPLEX WITH COPPER, FUNCTION, COFACTOR, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=8204598; DOI=10.1021/bi00187a031;
RA   Bagby S., Driscoll P.C., Harvey T.S., Hill H.A.O.;
RT   "High-resolution solution structure of reduced parsley plastocyanin.";
RL   Biochemistry 33:6611-6622(1994).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:8204598}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:8204598};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:8204598, ECO:0000269|Ref.2}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:8204598}; Lumenal side
CC       {ECO:0000269|PubMed:8204598}. Note=Loosely bound to the inner thylakoid
CC       membrane surface in chloroplasts (PubMed:8204598).
CC   -!- MISCELLANEOUS: The sequence shown is that of plastocyanin A. There is
CC       only 1 difference between the sequence of parsley plastocyanins A and
CC       B.
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR   PIR; JW0014; JW0014.
DR   PDB; 1PLA; NMR; -; A=1-97.
DR   PDB; 1PLB; NMR; -; A=1-97.
DR   PDBsum; 1PLA; -.
DR   PDBsum; 1PLB; -.
DR   AlphaFoldDB; P17341; -.
DR   SMR; P17341; -.
DR   EvolutionaryTrace; P17341; -.
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..97
FT                   /note="Plastocyanin A/B"
FT                   /id="PRO_0000085570"
FT   DOMAIN          1..97
FT                   /note="Plastocyanin-like"
FT   BINDING         37
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:8204598"
FT   BINDING         82
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:8204598"
FT   BINDING         85
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:8204598"
FT   BINDING         90
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:8204598"
FT   VARIANT         53
FT                   /note="E -> D (in plastocyanin B)"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          14..21
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:1PLB"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:1PLA"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:1PLA"
SQ   SEQUENCE   97 AA;  10290 MW;  13B76E4BA5AB54DF CRC64;
     AEVKLGSDDG GLVFSPSSFT VAAGEKITFK NNAGFPHNIV FDEDEVPAGV NAEKISQPEY
     LNGAGETYEV TLTEKGTYKF YCEPHAGAGM KGEVTVN
 
 
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