UCRIA_BIGNA
ID UCRIA_BIGNA Reviewed; 252 AA.
AC Q7XYM4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS CCMP621)).
OC Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX NCBI_TaxID=227086;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12777624; DOI=10.1073/pnas.1230951100;
RA Archibald J.M., Rogers M.B., Toop M., Ishida K., Keeling P.J.;
RT "Lateral gene transfer and the evolution of plastid-targeted proteins in
RT the secondary plastid-containing alga Bigelowiella natans.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7678-7683(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 {ECO:0000250}.
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The
CC transmembrane helix obliquely spans the membrane in one monomer, and
CC its extrinsic C-terminal domain is part of the other monomer.
CC {ECO:0000250}.
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}.
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DR EMBL; AY267656; AAP79170.1; -; mRNA.
DR AlphaFoldDB; Q7XYM4; -.
DR SMR; Q7XYM4; -.
DR STRING; 227086.JGI_V11_47452; -.
DR OMA; KGDPTYI; -.
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:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW 2Fe-2S; Chloroplast; Disulfide bond; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Plastid; Thylakoid; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..252
FT /note="Cytochrome b6-f complex iron-sulfur subunit,
FT chloroplastic"
FT /id="PRO_0000030686"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 141..235
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 181
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 183
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 199
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 202
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 186..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 252 AA; 26862 MW; 9BDD2C12697EF92A CRC64;
MAQSRSLLLS IAVNALLVGV LLYSVAVNRT QEGSLQLSAV RGKIAAPRTS FQNAVSRVSR
NQLPSSSRKA VAQAFLSNPD MVPDMGKRKL MNNLVLAAVA PVVASAGGCY LYYFYPPQTG
GGGGAVGALD ALGNPVSAES WFKSHKKNAR DLVQGIKGDP TYLIVNDDGS TLNSYGLNAI
CTHLGCVVPW DAASNKFKCP CHGSQYAPDG HVVRGPAPRP LQLAHVEDDN GKILLSPWTE
TDFRTGEKPW WA
