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UniProtKB/Swiss-Prot entry Q8KPS9


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

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Entry information
Entry name PCYA_SYNE7
Primary accession number Q8KPS9
Secondary accession number Q31NW4
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 26)
Name and origin of the protein
Protein name Phycocyanobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.5
Gene name
Name: pcyA
OrderedLocusNames: Synpcc7942_1225
ORFNames: see0002
From
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [TaxID: 1140] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S., Gonzalez A., Salinas I., Golden S.S., Youderian P.;
"Synechococcus elongatus PCC7942 cosmid 7G3.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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
AY120853; AAM82675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000100; ABB57255.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_400242.1; -.
3D structure databases
ModBase Q8KPS9.
Enzyme and pathway databases
BioCyc SELO1140:SYNPCC7942_1225-MON; -.
Ontologies
GO
GO:0050897; Molecular function: cobalt ion binding (inferred from electronic annotation from InterPro).
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).
GO:0010024; Biological process: phytochromobilin biosynthetic process (inferred from electronic annotation from InterPro).
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.
ProtoNet Q8KPS9.
Genome annotation databases
GeneID 3773513; -.
GenomeReviews CP000100_GR; Synpcc7942_1225.
KEGG syf:Synpcc7942_1225; -.
Phylogenomic databases
HOGENOM Q8KPS9; -.
Genome annotation databases
CMR Q8KPS9; Synpcc7942_1225.
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   248  248     Phycocyanobilin:ferredoxin oxidoreductase. PRO_0000216745
Sequence information
Length: 248 AA [This is the length of the unprocessed precursor] Molecular weight: 27987 Da [This is the MW of the unprocessed precursor] CRC64: 4C824F0F6FECD8DA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSSTQVGLK EQLHPLIRDL ATGIEATWQR WLNLEPYAAM PADLGYIEGK LEGERLQIEN 

        70         80         90        100        110        120 
RCYQSREFRK LHLELARVGN NLDILHCVLF PRTTFDLPMF GADLVGGRGQ ISAAIVDLSP 

       130        140        150        160        170        180 
TTIARELSND YIAGLTALPN PTFQGLRELP TWGDIFSSFC LFIRPGSPEE EAAFLDRALG 

       190        200        210        220        230        240 
FLQVHCQQAA AATALTDPEA IATVLEQQRY YCEQQRRNDK TRRVLEKAFG DDWADRYMTT 


MLFDLPSD 

Q8KPS9 in FASTA format

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