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UniProtKB/Swiss-Prot entry Q93TN0

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

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Entry information
Entry name PCYA_ANASP
Primary accession number Q93TN0
Secondary accession numbers None
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 34)
Name and origin of the protein
Protein name Phycocyanobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.5
Gene name
Name: pcyA
OrderedLocusNames: alr3707
From
Anabaena sp. (strain PCC 7120) [TaxID: 103690] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1105/tpc.13.4.965; PubMed=11283349 [NCBI, ExPASy, EBI, Israel, Japan]
Frankenberg N., Mukougawa K., Kohchi T., Lagarias J.C.;
"Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms.";
Plant Cell 13:965-978(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/8.5.205; PubMed=11759840 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., Yasuda M., Tabata S.;
"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120.";
DNA Res. 8:205-213(2001).
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.
  • 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
AF339056; AAK38587.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000019; BAB75406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR AD2269; AD2269.
RefSeq NP_487747.1; -.
3D structure databases
PDB
2G18; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-245.[ExPASy / RCSB / EBI]
PDBsum 2G18; -.
ModBase Q93TN0.
Enzyme and pathway databases
BioCyc NSP103690:ALR3707-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 Q93TN0.
Genome annotation databases
GeneID 1107305; -.
GenomeReviews BA000019_GR; alr3707.
KEGG ana:alr3707; -.
NMPDR fig|103690.1.peg.4014; -.
Phylogenomic databases
HOGENOM Q93TN0; -.
Genome annotation databases
CMR Q93TN0; alr3707.
Other
ProtoNet Q93TN0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   245  245     Phycocyanobilin:ferredoxin oxidoreductase. PRO_0000216738
STRAND   3     7  5      
HELIX   9    12  4      
HELIX   15    31  17      
HELIX   41    43  3      
STRAND   44    50  7      
STRAND   53    63  11      
STRAND   65    77  13      
TURN   78    80  3      
STRAND   81    90  10      
STRAND   98   106  9      
STRAND   109   118  10      
HELIX   128   136  9      
STRAND   143   145  3      
HELIX   152   154  3      
STRAND   160   162  3      
HELIX   167   190  24      
HELIX   196   216  21      
HELIX   219   227  9      
HELIX   229   238  10      
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 27959 Da [This is the MW of the unprocessed precursor] CRC64: 8F6CE652EFEE011A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSLTSIPSLR EQQHPLIRQL ADCIEEVWHQ HLDLSPYHLP AELGYVEGRL EGEKLTIENR 

        70         80         90        100        110        120 
CYQTPQFRKM HLELAKVGNM LDILHCVMFP RPEYDLPMFG CDLVGGRGQI SAAIADLSPV 

       130        140        150        160        170        180 
HLDRTLPESY NSALTSLNTL NFSQPRELPE WGNIFSDFCI FVRPSSPEEE AMFLGRVREF 

       190        200        210        220        230        240 
LQVHCQGAIA ASPVSAEQKQ QILAGQHNYC SKQQQNDKTR RVLEKAFGVD WAENYMTTVL 


FDLPE
Q93TN0 in FASTA format

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