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UniProtKB/Swiss-Prot entry A2CA92


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

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Entry information
Entry name PCYA_PROM3
Primary accession number A2CA92
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on February 20, 2007 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 11)
Name and origin of the protein
Protein name Phycocyanobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.5
Gene name
Name: pcyA
OrderedLocusNames: P9303_16581
From
Prochlorococcus marinus (strain MIT 9303) [TaxID: 59922] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0030231; PubMed=18159947 [NCBI, ExPASy, EBI, Israel, Japan]
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.;
"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus.";
PLoS Genet. 3:2515-2528(2007).
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
CP000554; ABM78402.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001017667.1; -.
3D structure databases
ModBase A2CA92.
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 A2CA92.
Genome annotation databases
GeneID 4777227; -.
GenomeReviews CP000554_GR; P9303_16581.
KEGG pmf:P9303_16581; -.
CMR A2CA92; P9303_16581.
Other
ProtoNet A2CA92.
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_1000061375
Sequence information
Length: 264 AA [This is the length of the unprocessed precursor] Molecular weight: 29034 Da [This is the MW of the unprocessed precursor] CRC64: ACA70C077F034E79 [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 CRGLRKLHLE IARLGGGLQV LHCVFFPDPR FDLPIFGADI 

       130        140        150        160        170        180 
VASPAGISAA IVDLSPVGLT MPVALLHGLE SLPIPAFQQV RELPAWGSIF SPFVQFIRPA 

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

       250        260 
EKAFNPQWAD RYIEEILFED PPPL 

A2CA92 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
NPSA logo NPSA Sequence analysis tools

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