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UniProtKB/Swiss-Prot entry Q02190


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

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Entry information
Entry name PEBB_SYNPY
Primary accession number Q02190
Secondary accession number Q93MM9
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on February 12, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 32)
Name and origin of the protein
Protein name Phycoerythrobilin:ferredoxin oxidoreductase
Synonym EC 1.3.7.3
Gene name
Name: pebB
From
Synechococcus sp. (strain WH8020) [TaxID: 32052] 
Taxonomy Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00019939; PubMed=8425055 [NCBI, ExPASy, EBI, Israel, Japan]
de Lorimier R., Wilbanks S.M., Glazer A.N.;
"Genes of the R-phycocyanin II locus of marine Synechococcus spp., and comparison of protein-chromophore interactions in phycocyanins differing in bilin composition.";
Plant Mol. Biol. 21:225-237(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8419325 [NCBI, ExPASy, EBI, Israel, Japan]
Wilbanks S.M., Glazer A.N.;
"Rod structure of a phycoerythrin II-containing phycobilisome. I. Organization and sequence of the gene cluster encoding the major phycobiliprotein rod components in the genome of marine Synechococcus sp. WH8020.";
J. Biol. Chem. 268:1226-1235(1993).
[3]
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).
Comments
  • FUNCTION: Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin.
  • CATALYTIC ACTIVITY: (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + 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
M95288; AAA27344.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF400985; AAK77916.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B46448; B46448.
3D structure databases
ModBase Q02190.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13952; -.
Ontologies
GO
GO:0050897; Molecular function: cobalt ion binding (inferred from electronic annotation from InterPro).
GO:0050618; Molecular function: phycoerythrobilin: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_00793; -; 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 Q02190.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   257  257     Phycoerythrobilin:ferredoxin oxidoreductase. PRO_0000216737
CONFLICT   100   100        D -> G (in Ref. 1 and 2). 
CONFLICT   111   111        L -> F (in Ref. 1 and 2). 
Sequence information
Length: 257 AA [This is the length of the unprocessed precursor] Molecular weight: 29289 Da [This is the MW of the unprocessed precursor] CRC64: 26D65B6E8E7BFE8C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTNQRFKSTD PVNIEGWSWQ PFLEDAIKRL EGLNVEPYPV PDRFLQREDQ TGSKSKSIPV 

        70         80         90        100        110        120 
TTATWACKTE KFRQVRAACV SAGSAASVLN FVINPKSTYD LPFFGGDLVT LPAGHLLALD 

       130        140        150        160        170        180 
LQPAIKTDEV HTTHVWDRLI PIFERWRDQL PYGGPIPEEA QPFFSPGFLW TRLPLGEEGD 

       190        200        210        220        230        240 
ELIQSIVRPA FNDYLDLYLE LAASAERVTD ERSEVLLQGQ RKYTDYRAEK DPARGMLTRF 

       250 
HGSEWTEAYI HTVLFDL 

Q02190 in FASTA format

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