PLAS_TRIV2
ID PLAS_TRIV2 Reviewed; 139 AA.
AC Q3M9H8; P00301; P14114;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Plastocyanin;
DE Flags: Precursor;
GN Name=petE; Synonyms=petE1; OrderedLocusNames=Ava_2745;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2501629; DOI=10.1111/j.1365-2958.1989.tb00172.x;
RA van de Plas J., Bovy A., Kruyt F., de Vrieze G., Dassen E., Klein B.,
RA Weisbeek P.J.;
RT "The gene for the precursor of plastocyanin from the cyanobacterium
RT Anabaena sp. PCC 7937: isolation, sequence and regulation.";
RL Mol. Microbiol. 3:275-284(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
RN [3]
RP PROTEIN SEQUENCE OF 35-139, AND SUBCELLULAR LOCATION.
RX PubMed=812489; DOI=10.1042/bj1490675;
RA Aitken A.;
RT "Prokaryote-eukaryote relationship and the amino acid sequence of
RT plastocyanin from Anabaena variabilis.";
RL Biochem. J. 149:675-683(1975).
RN [4]
RP STRUCTURE BY NMR OF 35-138 IN COMPLEX WITH COPPER, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RX DOI=10.1021/ja001368z;
RA Ma L., Jorgensen A.M., Soerensen G.O., Ulstrup J., Led J.J.;
RT "Elucidation of the paramagnetic R1 relaxation of heteronuclei and protons
RT in Cu(II) plastocyanin from Anabaena variabilis.";
RL J. Am. Chem. Soc. 122:9473-9485(2000).
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:0000255|HAMAP-Rule:MF_00566, ECO:0000269|Ref.4};
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00566, ECO:0000269|PubMed:812489, ECO:0000269|Ref.4};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00566}; Lumenal
CC side {ECO:0000255|HAMAP-Rule:MF_00566}. Note=Loosely bound to the
CC thylakoid inner membrane surface.
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC Rule:MF_00566}.
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DR EMBL; X14342; CAA32527.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA22358.1; -; Genomic_DNA.
DR PDB; 1FA4; NMR; -; A=35-138.
DR PDBsum; 1FA4; -.
DR AlphaFoldDB; Q3M9H8; -.
DR BMRB; Q3M9H8; -.
DR SMR; Q3M9H8; -.
DR STRING; 240292.Ava_2745; -.
DR EnsemblBacteria; ABA22358; ABA22358; Ava_2745.
DR KEGG; ava:Ava_2745; -.
DR eggNOG; COG3794; Bacteria.
DR HOGENOM; CLU_084115_0_1_3; -.
DR OMA; YDYYCEP; -.
DR EvolutionaryTrace; Q3M9H8; -.
DR Proteomes; UP000002533; Chromosome.
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; Direct protein sequencing; Electron transport;
KW Membrane; Metal-binding; Signal; Thylakoid; Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT CHAIN 35..139
FT /note="Plastocyanin"
FT /id="PRO_0000002900"
FT DOMAIN 35..135
FT /note="Plastocyanin-like"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 131
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|Ref.4"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1FA4"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1FA4"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1FA4"
SQ SEQUENCE 139 AA; 14635 MW; E5816E91576C6C66 CRC64;
MKLIAASLRR LSLAVLTVLL VVSSFAVFTP SAAAETYTVK LGSDKGLLVF EPAKLTIKPG
DTVEFLNNKV PPHNVVFDAT LNPAKSADLA KSLSHKQLLM SPGQSTSTTF PADAPAGDYS
FYCEPHRGAG MVGKITVAS
