UCRIA_CHLRE
ID UCRIA_CHLRE Reviewed; 206 AA.
AC P49728;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit, chloroplastic;
DE EC=7.1.1.6;
DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=ISP;
DE Short=RISP;
DE Flags: Precursor;
GN Name=petC;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cw15;
RX PubMed=8125984; DOI=10.1016/s0021-9258(17)37330-1;
RA de Vitry C.;
RT "Characterization of the gene of the chloroplast Rieske iron-sulfur protein
RT in Chlamydomonas reinhardtii. Indications for an uncleaved lumen targeting
RT sequence.";
RL J. Biol. Chem. 269:7603-7609(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2137;
RA Takahashi Y., Kataoka S., Matsubara H., Malkin R.;
RT "A cDNA encoding chloroplast Rieske protein from Chlamydomonas
RT reinhardtii.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 30-56 AND 168-186, AND CHARACTERIZATION.
RC STRAIN=WT12;
RX PubMed=7493968; DOI=10.1074/jbc.270.49.29342;
RA Pierre Y., Breyton C., Kramer D., Popot J.-L.;
RT "Purification and characterization of the cytochrome b6 f complex from
RT Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 270:29342-29349(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-206.
RX PubMed=14647374; DOI=10.1038/nature02155;
RA Stroebel D., Choquet Y., Popot J.-L., Picot D.;
RT "An atypical haem in the cytochrome b(6)f complex.";
RL Nature 426:413-418(2003).
CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC electron transfer between photosystem II (PSII) and photosystem I
CC (PSI), cyclic electron flow around PSI, and state transitions.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster per subunit.;
CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC the Rieske protein, while the 4 small subunits are petG, petL, petM and
CC petN. The complex functions as a dimer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-
CC pass membrane protein. Note=The transmembrane helix obliquely spans the
CC membrane in one monomer, and its extrinsic C-terminal domain is part of
CC the other monomer.
CC -!- MISCELLANEOUS: This protein is 1 of 2 subunits of the cytochrome b6-f
CC complex that are encoded in the nucleus.
CC -!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe-
CC 2S protein.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X76299; CAA53947.1; -; Genomic_DNA.
DR EMBL; D32003; BAA22147.1; -; mRNA.
DR PIR; A53412; A53412.
DR RefSeq; XP_001698786.1; XM_001698734.1.
DR PDB; 1Q90; X-ray; 3.10 A; C=80-206, R=31-79.
DR PDBsum; 1Q90; -.
DR AlphaFoldDB; P49728; -.
DR SMR; P49728; -.
DR DIP; DIP-58594N; -.
DR IntAct; P49728; 2.
DR STRING; 3055.EDO99286; -.
DR EnsemblPlants; PNW76554; PNW76554; CHLRE_11g467689v5.
DR GeneID; 5724296; -.
DR Gramene; PNW76554; PNW76554; CHLRE_11g467689v5.
DR eggNOG; KOG1671; Eukaryota.
DR HOGENOM; CLU_055690_8_0_1; -.
DR OMA; KGDPTYI; -.
DR OrthoDB; 1361271at2759; -.
DR BioCyc; MetaCyc:CHLREDRAFT_193296-MON; -.
DR EvolutionaryTrace; P49728; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010196; P:nonphotochemical quenching; IEA:EnsemblPlants.
DR Gene3D; 2.102.10.10; -; 1.
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; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Chloroplast; Direct protein sequencing;
KW Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Plastid; Thylakoid; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..29
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:7493968"
FT CHAIN 30..206
FT /note="Cytochrome b6-f complex iron-sulfur subunit,
FT chloroplastic"
FT /id="PRO_0000030685"
FT TRANSMEM 39..68
FT /note="Helical"
FT DOMAIN 92..188
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 134
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 152
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 155
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT DISULFID 139..154
FT HELIX 39..68
FT /evidence="ECO:0007829|PDB:1Q90"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1Q90"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1Q90"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1Q90"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1Q90"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1Q90"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1Q90"
SQ SEQUENCE 206 AA; 21526 MW; 7B2C2118E9F75974 CRC64;
MAMLSSRRVA APAKASAIRR SRVMPVVRAA AASSEVPDMN KRNIMNLILA GGAGLPITTL
ALGYGAFFVP PSSGGGGGGQ AAKDALGNDI KAGEWLKTHL AGDRSLSQGL KGDPTYLIVT
ADSTIEKYGL NAVCTHLGCV VPWVAAENKF KCPCHGSQYN AEGKVVRGPA PLSLALAHCD
VAESGLVTFS TWTETDFRTG LEPWWA
