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UniProtKB/Swiss-Prot entry Q7VCC2


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

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Entry information
Entry name PCYA_PROMA
Primary accession number Q7VCC2
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 23)
Name and origin of the protein
Protein name Phycocyanobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.5
Gene name
Name: pcyA
OrderedLocusNames: Pro_0819
From
Prochlorococcus marinus [TaxID: 1219] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SARG / CCMP1375 / SS120;
DOI=10.1073/pnas.1733211100; PubMed=12917486 [NCBI, ExPASy, EBI, Israel, Japan]
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome.";
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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
AE017126; AAP99863.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_875211.1; -.
3D structure databases
ModBase Q7VCC2.
Enzyme and pathway databases
BioCyc PMAR167539:PRO_0819-MON; -.
Ontologies
GO
GO:0050620; Molecular function: phycocyanobilin:ferredoxin oxidoreductase activity (inferred from electronic annotation from HAMAP).
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 Q7VCC2.
Genome annotation databases
GeneID 1462201; -.
GenomeReviews AE017126_GR; Pro_0819.
KEGG pma:Pro0819; -.
Phylogenomic databases
HOGENOM Q7VCC2; -.
Genome annotation databases
CMR Q7VCC2; Pro_0819.
Other
ProtoNet Q7VCC2.
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   247  247     Phycocyanobilin:ferredoxin oxidoreductase. PRO_0000216741
Sequence information
Length: 247 AA [This is the length of the unprocessed precursor] Molecular weight: 28253 Da [This is the MW of the unprocessed precursor] CRC64: 86C0ACBF02A31993 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFAKSFPLNP FLESVADRIR ERVKGLTGVE SLELAPDLKN IYGKTDGEDF FIFNELHQSR 

        70         80         90        100        110        120 
GFRKLHIETA VFEPSLEILH VVFFPDPAFD LPIFGVDLIA VPQGISAAIV DLSPVRDKLP 

       130        140        150        160        170        180 
RTIENQLAQI EIPSFEKVRK LPDWGDIFSS HVQFITPIGA EENGFFLDLV DKFLTILIDY 

       190        200        210        220        230        240 
SESIEPDLDD SPFTIERIEG QMYYCLQQKQ NDKTRNVLAK AFSPNWANQY IEMVLFDMPV 


HTKNLDN 

Q7VCC2 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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