UCRIA_SYNY3
ID UCRIA_SYNY3 Reviewed; 178 AA.
AC P74714;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit 1 {ECO:0000255|HAMAP-Rule:MF_01335};
DE EC=7.1.1.6 {ECO:0000255|HAMAP-Rule:MF_01335};
DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein 1 {ECO:0000255|HAMAP-Rule:MF_01335};
DE Short=ISP 1 {ECO:0000255|HAMAP-Rule:MF_01335};
DE Short=RISP 1 {ECO:0000255|HAMAP-Rule:MF_01335};
DE AltName: Full=Rieske iron-sulfur protein 1 {ECO:0000255|HAMAP-Rule:MF_01335};
GN Name=petC1 {ECO:0000255|HAMAP-Rule:MF_01335}; OrderedLocusNames=slr1185;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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:0000255|HAMAP-Rule:MF_01335}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01335};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01335};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01335};
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. {ECO:0000255|HAMAP-
CC Rule:MF_01335}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01335}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01335}. 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. {ECO:0000255|HAMAP-Rule:MF_01335}.
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:0000255|HAMAP-Rule:MF_01335}.
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DR EMBL; BA000022; BAA18833.1; -; Genomic_DNA.
DR PIR; S76921; S76921.
DR AlphaFoldDB; P74714; -.
DR SMR; P74714; -.
DR IntAct; P74714; 1.
DR STRING; 1148.1653923; -.
DR TCDB; 3.D.3.5.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P74714; -.
DR EnsemblBacteria; BAA18833; BAA18833; BAA18833.
DR KEGG; syn:slr1185; -.
DR eggNOG; COG0723; Bacteria.
DR InParanoid; P74714; -.
DR OMA; QIFISPW; -.
DR PhylomeDB; P74714; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.102.10.10; -; 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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..178
FT /note="Cytochrome b6-f complex iron-sulfur subunit 1"
FT /id="PRO_0000127784"
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT DOMAIN 61..161
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 125
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 128
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT DISULFID 112..127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
SQ SEQUENCE 178 AA; 18685 MW; 6AFF9F4195A61956 CRC64;
MDNTQAIAPP SYSRRQLLNF LAGTTVAVTA SAGAYAMGKF FVPPAEKGGA GGGIIAKDVL
GNPIPASQIL AEAPGTRALV AGLAGDPTYL IVKEDGSLDS IGIVDSCTHL GCTFPWNGND
QEFQCPCHGS RYHPDGSVAR GPAPLPLKIV QVAVVDDQIF ISPWTDLDPR TGEKPWWV
