ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P26292


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name UCRI_SYNP2
Primary accession number P26292
Secondary accession number B1XQK1
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name Cytochrome b6-f complex iron-sulfur subunit
Synonyms EC 1.10.99.1
Rieske iron-sulfur protein
Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein
ISP
RISP
Gene name
Name: petC
OrderedLocusNames: SYNPCC7002_A1909
From
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [TaxID: 32049] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00040607; PubMed=1421151 [NCBI, ExPASy, EBI, Israel, Japan]
Brand S.N., Tan X., Widger W.R.;
"Cloning and sequencing of the petBD operon from the cyanobacterium Synechococcus sp. PCC 7002.";
Plant Mol. Biol. 20:481-491(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
"Complete sequence of Synechococcus sp. PCC 7002.";
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
Comments
  • FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity).
  • CATALYTIC ACTIVITY: Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin.
  • COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
  • SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).
  • SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein (By similarity). Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer (By similarity).
  • MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe-2S protein.
  • SIMILARITY: Contains 1 Rieske domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M74514; AAA22069.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000951; ACA99896.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001735152.1; -.
3D structure databases
HSSP P08980; 1RFS. [HSSP ENTRY / PDB]
ModBase P26292.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042651; Cellular component: thylakoid membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0045158; Molecular function: electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity (inferred from electronic annotation from HAMAP).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009496; Molecular function: plastoquinol-plastocyanin reductase activity (inferred from electronic annotation from HAMAP).
GO:0008121; Molecular function: ubiquinol-cytochrome-c reductase activity (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0015979; Biological process: photosynthesis (inferred from electronic annotation from HAMAP).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01335; -; 1.
PBIL [Tree]
InterPro IPR014909; Cyt_b6-F_Fe-S_su.
IPR014349; Rieske.
IPR005805; Rieske_C.
IPR005806; Rieske_reg.
Graphical view of domain structure.
Gene3D G3DSA:2.102.10.10; Rieske_reg; 1.
PANTHER PTHR10134; Rieske; 1.
Pfam PF08802; CytB6-F_Fe-S; 1.
PF00355; Rieske; 1.
Pfam graphical view of domain structure.
PRINTS PR00162; RIESKE.
PROSITE PS51296; RIESKE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P26292.
ProtoNet P26292.
Genome annotation databases
GeneID 6057819; -.
GenomeReviews CP000951_GR; SYNPCC7002_A1909.
KEGG syp:SYNPCC7002_A1909; -.
CMR P26292; SYNPCC7002_A1909.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Complete proteome; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Thylakoid; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   180  180     Cytochrome b6-f complex iron-sulfur subunit. PRO_0000127781
TRANSMEM   21    43  23     Potential. 
DOMAIN   70   162  93     Rieske. 
METAL   108   108        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   110   110        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   126   126        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   129   129        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
DISULFID   113   128        By similarity. 
Sequence information
Length: 180 AA [This is the length of the unprocessed precursor] Molecular weight: 19178 Da [This is the MW of the unprocessed precursor] CRC64: 7A8185C310B47917 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTQLSGSSDV PDLGRRQFLN LLWVGTAAGT ALGGLYPVIK YFIPPSSGGA GGGVIAKDAL 

        70         80         90        100        110        120 
GNDIIVSDYL QTHTAGDRSL AQGLKGDPTY VVVEGDNTIS SYGINAICTH LGCVVPWNTA 

       130        140        150        160        170        180 
ENKFMCPCHG SQYDETGKVV RGPAPLSLAL VHAEVTEDDK ISFTDWTETD FRTDEAPWWA 

P26292 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!