Reviewed, UniProtKB/Swiss-Prot Q02190 (PEBB_SYNPY)

Names and origin

Protein names

Recommended name:
    Phycoerythrobilin:ferredoxin oxidoreductase
    EC=1.3.7.3

Gene names

Name:

pebB

Organism

Synechococcus sp. (strain WH8020)

Taxonomic identifier

32052 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. HAMAP MF_00793
Catalytic activity	(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin. HAMAP MF_00793
Sequence similarities	Belongs to the HY2 family.

Ontologies

Keywords
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phytochromobilin biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	cobalt ion binding Inferred from electronic annotation. Source: InterPro phycoerythrobilin:ferredoxin oxidoreductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 257	257	Phycoerythrobilin:ferredoxin oxidoreductase HAMAP MF_00793		PRO_0000216737
Experimental info
	Sequence conflict	100	1	D → G Ref.1
	Sequence conflict	100	1	D → G Ref.2
	Sequence conflict	111	1	L → F Ref.1
	Sequence conflict	111	1	L → F Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q02190-1 [UniParc]. Last modified February 12, 2003. Version 2. Checksum: 26D65B6E8E7BFE8C	FASTA	257	29,289
	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

References

[1]	"Genes of the R-phycocyanin II locus of marine Synechococcus spp., and comparison of protein-chromophore interactions in phycocyanins differing in bilin composition." de Lorimier R., Wilbanks S.M., Glazer A.N. Plant Mol. Biol. 21:225-237(1993) [PubMed: 8425055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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." Wilbanks S.M., Glazer A.N. J. Biol. Chem. 268:1226-1235(1993) [PubMed: 8419325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms." Frankenberg N., Mukougawa K., Kohchi T., Lagarias J.C. Plant Cell 13:965-978(2001) [PubMed: 11283349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M95288 Genomic DNA. Translation: AAA27344.1. AF400985 Genomic DNA. Translation: AAK77916.1.
PIR	B46448.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13952.
Family and domain databases
HAMAP	MF_00793. [Tree]
InterPro	IPR009249. Ferredoxin-dep_bilin_Rdtase. [Graphical view]
Pfam	PF05996. Fe_bilin_red. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEBB_SYNPY

Accession

Primary (citable) accession number: Q02190
Secondary accession number(s): Q93MM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 12, 2003
Last modified:	March 3, 2009
This is version 33 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)