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 P59288


[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 PCYA_SYNEL
Primary accession number P59288
Secondary accession numbers None
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on February 12, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 28)
Name and origin of the protein
Protein name Phycocyanobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.5
Gene name
Name: pcyA
OrderedLocusNames: tll2308
From
Synechococcus elongatus (Thermosynechococcus elongatus) [TaxID: 32046] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
DOI=10.1093/dnares/9.4.123; PubMed=12240834 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
Comments
  • FUNCTION: Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin (By similarity).
  • CATALYTIC ACTIVITY: (3Z)-phycocyanobilin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin.
  • SIMILARITY: Belongs to the HY2 family.
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
BA000039; BAC09860.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_683098.1; -.
3D structure databases
ModBase P59288.
Enzyme and pathway databases
BioCyc TELO197221:TLL2308-MON; -.
Ontologies
GO
GO:0050620; Molecular function: phycocyanobilin:ferredoxin oxidoreductase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00618; -; 1.
PBIL [Tree]
InterPro IPR009249; Fe_bilin_red.
Graphical view of domain structure.
Pfam PF05996; Fe_bilin_red; 1.
Pfam graphical view of domain structure.
BLOCKS P59288.
ProtoNet P59288.
Genome annotation databases
GeneID 1012200; -.
GenomeReviews BA000039_GR; tll2308.
KEGG tel:tll2308; -.
NMPDR fig|197221.1.peg.2307; -.
Phylogenomic databases
HOGENOM P59288; -.
Genome annotation databases
CMR P59288; tll2308.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   236  236     Phycocyanobilin:ferredoxin oxidoreductase. PRO_0000216744
Sequence information
Length: 236 AA [This is the length of the unprocessed precursor] Molecular weight: 26930 Da [This is the MW of the unprocessed precursor] CRC64: 359338886E898FBD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLRQHQHPL IQRLADRIEA IWQAFFPLAP YALPEDLGYV EGKLEGERLT IENHCYQAPP 

        70         80         90        100        110        120 
FRKLHLELAR VGESLDILHC VMFPEPRYDL PMFGCDLVGG RGQISAAIVD LSPVTGQLPA 

       130        140        150        160        170        180 
AYTCALNALP KLTFRQPREL PPWGHIFSPF CIFIRPQGEA EEQQFLDRIG EYLTLHCQLS 

       190        200        210        220        230 
QQAVPTDHPQ AVIAGQRQYC QQQQQNDKTR RVLEKAFGVP WAERYMTTVL FDVPPV 

P59288 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!