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Database: UniProt
Entry: A5BX41_VITVI
LinkDB: A5BX41_VITVI
Original site: A5BX41_VITVI 
ID   A5BX41_VITVI            Unreviewed;       228 AA.
AC   A5BX41;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=plastoquinol--plastocyanin reductase {ECO:0000256|ARBA:ARBA00012952};
DE            EC=7.1.1.6 {ECO:0000256|ARBA:ARBA00012952};
GN   OrderedLocusNames=VIT_19s0014g03850 {ECO:0000313|EMBL:CBI20394.3};
GN   ORFNames=VITISV_020089 {ECO:0000313|EMBL:CAN66108.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN66108.1};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
RN   [2] {ECO:0000313|EMBL:CAN66108.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT   vinifera L.): coping with a highly heterozygous genome.";
RL   PLoS ONE 2:e1326-e1326(2007).
RN   [3] {ECO:0000313|EMBL:CBI20394.3}
RP   NUCLEOTIDE SEQUENCE.
RA   Vitulo N., Olivier J., Forcato C., Albiero A., D'Angelo M., Zimbello R.,
RA   Schiavon R., Rigobello C., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Vezzi A., Hugueney P., Horner D., Mica E., Cattonaro F.,
RA   Del Fabbro C., Alaux M., Di Gaspero G., Scalabrin S., Pesole G.,
RA   Delledonne M., Pezzotti M., Pe E.M., Caboche M., Adam-Blondon A.-F.,
RA   Weissenbach J., Quetier F., Wincker P., Morgante M., Valle G.;
RT   "High quality assembly and annotation of grapevine genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a
CC         plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin];
CC         Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC         Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:62192; EC=7.1.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000603};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000256|ARBA:ARBA00010651}.
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DR   EMBL; AM474316; CAN66108.1; -; Genomic_DNA.
DR   EMBL; FN595229; CBI20394.3; -; Genomic_DNA.
DR   RefSeq; XP_002284361.1; XM_002284325.3.
DR   AlphaFoldDB; A5BX41; -.
DR   STRING; 29760.A5BX41; -.
DR   PaxDb; 29760-VIT_19s0014g03850-t01; -.
DR   EnsemblPlants; Vitvi19g00308_t001; Vitvi19g00308_P001; Vitvi19g00308.
DR   GeneID; 100258879; -.
DR   Gramene; Vitvi19g00308_t001; Vitvi19g00308_P001; Vitvi19g00308.
DR   KEGG; vvi:100258879; -.
DR   eggNOG; KOG1671; Eukaryota.
DR   HOGENOM; CLU_055690_8_0_1; -.
DR   OMA; PFNSAEN; -.
DR   OrthoDB; 275935at2759; -.
DR   Proteomes; UP000009183; Chromosome 19.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd03471; Rieske_cytochrome_b6f; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   Gene3D; 1.20.5.700; Single helix bin; 1.
DR   HAMAP; MF_01335; Cytb6_f_Rieske; 1.
DR   InterPro; IPR023960; Cyt_b6_f_Rieske.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10134:SF50; CYTOCHROME B6-F COMPLEX IRON-SULFUR SUBUNIT, CHLOROPLASTIC; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        67..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..211
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   228 AA;  24076 MW;  AF22DCB12BFFA539 CRC64;
     MAASTLSPAT SSQLCSIRNG VLSPSHALLP KLTRTSPFVG KGKGLKIKCQ ATSIPADRVP
     DMGKRKLMNL LLLGAISLPS AGMLIPYATF FAPPGTGSAG GGIVAKDALG NDVIADEWLK
     THGPGDRTLT QGLKGDPTYL VVENDKTLAT YGINAVCTHL GCVVPWNAAE NKFICPCHGS
     QYNNQGRVVR GPAPLSLALA HADIDDGKVL FVPWVETDFR TGEDPWWA
//
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