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UniProtKB/Swiss-Prot entry Q7V7Y8


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

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Entry information
Entry name PCYA_PROMM
Primary accession number Q7V7Y8
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 20)
Name and origin of the protein
Protein name Phycocyanobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.5
Gene name
Name: pcyA
OrderedLocusNames: PMT0590
From
Prochlorococcus marinus (strain MIT 9313) [TaxID: 74547] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(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
BX572096; CAE20765.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_894423.1; -.
3D structure databases
ModBase Q7V7Y8.
Enzyme and pathway databases
BioCyc PMAR74547:PMT0590-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 Q7V7Y8.
Genome annotation databases
GeneID 1728679; -.
GenomeReviews BX548175_GR; PMT0590.
KEGG pmt:PMT0590; -.
NMPDR fig|74547.1.peg.590; -.
Phylogenomic databases
HOGENOM Q7V7Y8; -.
Genome annotation databases
CMR Q7V7Y8; PMT0590.
Other
ProtoNet Q7V7Y8.
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   264  264     Phycocyanobilin:ferredoxin oxidoreductase. PRO_0000216742
Sequence information
Length: 264 AA [This is the length of the unprocessed precursor] Molecular weight: 29109 Da [This is the MW of the unprocessed precursor] CRC64: 97864813D508BDBA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MERVRGACQS PILILLAIVL PFPSTSGPAI HPLIESLAAR IRQRRAQLPE LSPFALDSVM 

        70         80         90        100        110        120 
ESISGQLDGE ELLISNELHR CRGMRKLHLE IARLGGGLQV LHCVFFPDPR FDLPIFGADI 

       130        140        150        160        170        180 
VAGPAGISAA IVDLSPVGLT MPEALLHGLE SLPIPAFQQV RELPEWGSIF SPFVQFIRPA 

       190        200        210        220        230        240 
SSQEESWFVD LADGYLKALI SSVIDATPDA SDAASTIQRH KSQLSYCIQQ KRNDKTRGVL 

       250        260 
EKAFNPQWAD RYIEEILFED PPPL 

Q7V7Y8 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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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
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