UCRI_MASLA
ID UCRI_MASLA Reviewed; 179 AA.
AC P83794; Q5YJJ8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit;
DE EC=7.1.1.6;
DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
DE Short=ISP {ECO:0000303|PubMed:14526088};
DE Short=RISP;
DE AltName: Full=Rieske iron-sulfur protein;
GN Name=petC;
OS Mastigocladus laminosus (Fischerella sp.).
OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX NCBI_TaxID=83541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yan J., Zhang H., Cramer W.A.;
RT "Cloning and characterization of the petBD and petCA operon from the
RT thermophilic cyanobacterium Mastigocladus laminosus.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH 2FE-2S CLUSTER IN
RP CYTOCHROME B6-F COMPLEX, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RX PubMed=14526088; DOI=10.1126/science.1090165;
RA Kurisu G., Zhang H., Smith J.L., Cramer W.A.;
RT "Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning
RT the cavity.";
RL Science 302:1009-1014(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:0000305|PubMed:14526088}.
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:0000269|PubMed:14526088};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:14526088};
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:0000269|PubMed:14526088}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000305|PubMed:14526088}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14526088}. Note=The transmembrane helix obliquely
CC spans the membrane in one monomer, and its extrinsic C-terminal domain
CC is part of the other monomer (PubMed:14526088).
CC {ECO:0000269|PubMed:14526088}.
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; AY390356; AAR26240.1; -; Genomic_DNA.
DR PDB; 1VF5; X-ray; 3.00 A; D/Q=1-179.
DR PDB; 2D2C; X-ray; 3.80 A; D/Q=1-179.
DR PDB; 2E74; X-ray; 3.00 A; D=1-179.
DR PDB; 2E75; X-ray; 3.55 A; D=1-179.
DR PDB; 2E76; X-ray; 3.41 A; D=1-179.
DR PDB; 4H0L; X-ray; 3.25 A; D=1-179.
DR PDB; 4H13; X-ray; 3.07 A; D=1-179.
DR PDB; 4I7Z; X-ray; 2.80 A; D=1-179.
DR PDB; 4PV1; X-ray; 3.00 A; D=1-179.
DR PDBsum; 1VF5; -.
DR PDBsum; 2D2C; -.
DR PDBsum; 2E74; -.
DR PDBsum; 2E75; -.
DR PDBsum; 2E76; -.
DR PDBsum; 4H0L; -.
DR PDBsum; 4H13; -.
DR PDBsum; 4I7Z; -.
DR PDBsum; 4PV1; -.
DR AlphaFoldDB; P83794; -.
DR SMR; P83794; -.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB04646; Dibromothymoquinone.
DR EvolutionaryTrace; P83794; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 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; Disulfide bond; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..179
FT /note="Cytochrome b6-f complex iron-sulfur subunit"
FT /id="PRO_0000127775"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TOPO_DOM 44..179
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:14526088"
FT DOMAIN 61..162
FT /note="Rieske"
FT /evidence="ECO:0000305|PubMed:14526088"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:14526088"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:14526088"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:14526088"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:14526088"
FT DISULFID 113..128
FT /evidence="ECO:0000269|PubMed:14526088"
FT CONFLICT 138
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 13..42
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4PV1"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2E74"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2E76"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2E74"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1VF5"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2E74"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2E74"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2E74"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1VF5"
SQ SEQUENCE 179 AA; 19401 MW; 3797DC66C5AFAD6C CRC64;
MAQFTESMDV PDMGRRQFMN LLAFGTVTGV ALGALYPLVK YFIPPSGGAV GGGTTAKDKL
GNNVKVSKFL ESHNAGDRVL VQGLKGDPTY IVVESKEAIR DYGINAVCTH LGCVVPWNAA
ENKFKCPCHG SQYDETGKVI RGPAPLSLAL CHATVQDDNI VLTPWTETDF RTGEKPWWV
