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 02-SEP-2026, entry version 165. 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=2 oxidized [plastocyanin] + a plastoquinol + 2 H(+)(in) = 2 CC reduced [plastocyanin] + a plastoquinone + 4 H(+)(out); 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 PDB; 1Q90; X-ray; 3.10 A; C=80-206, R=31-79. DR AlphaFoldDB; P49728; -. DR SMR; P49728; -. DR DIP; DIP-58594N; -. DR IntAct; P49728; 2. DR EnsemblPlants; PNW76554; PNW76554; CHLRE_11g467689v5. DR Gramene; PNW76554; PNW76554; CHLRE_11g467689v5. DR eggNOG; KOG1671; Eukaryota. DR HOGENOM; CLU_055690_8_0_1; -. DR OMA; FTPWTET; -. DR OrthoDB; 1637982at2759; -. DR BioCyc; CHLAMY:CHLREDRAFT_193296-MONOMER; -. DR BioCyc; MetaCyc:CHLREDRAFT_193296-MONOMER; -. DR EvolutionaryTrace; P49728; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblPlants. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants. DR GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC. DR CDD; cd03471; Rieske_cytochrome_b6f; 1. DR FunFam; 2.102.10.10:FF:000007; Cytochrome b6-f complex iron-sulfur subunit; 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 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 InterPro; IPR057415; TM_PetC. DR NCBIfam; NF010001; PRK13474.1; 1. DR PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF25471; TM_PetC; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; ISP domain; 1. DR SUPFAM; SSF81502; ISP transmembrane anchor; 1. DR PROSITE; PS51296; RIESKE; 1. DR PDBsum; 1Q90; -. 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..120 FT /evidence="ECO:0007829|PDB:1Q90" FT TURN 121..123 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 //