NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 7421;
DOI=10.1093/dnares/10.4.137; PubMed=14621292 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids.";
DNA Res. 10:137-145(2003).

Comments

FUNCTION: Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge (By similarity).
CATALYTIC ACTIVITY: 15,16-dihydrobiliverdin + 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

BA000045; BAC89201.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_924206.2; -.

3D structure databases

ModBase

Q7NL66.

Enzyme and pathway databases

BioCyc

GVIO251221:GLR1260-MON; -.

Ontologies

GO:0050617;	Molecular function: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00792; -; 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.

Genome annotation databases

GeneID

2598928; -.

GenomeReviews

BA000045_GR; glr1260.

KEGG

gvi:glr1260; -.

NMPDR

fig|251221.1.peg.1260; -.

Phylogenomic databases

HOGENOM

Q7NL66; -.

Genome annotation databases

CMR

Q7NL66; glr1260.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 244`	`244`		`15,16-dihydrobiliverdin:ferredoxin oxidoreductase.`	`PRO_0000216724`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 28515 Da [This is the MW of the unprocessed precursor]

CRC64: F45EAA4BB8294E1C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYRPFLEHLQ QKLQSSFDLQ SLTIPAGLDY RISERGREST TIRSWCYTCS ELRKIRYTYI 

        70         80         90        100        110        120 
DGGEHAQVFN SVIYPAHRYD LPLLGIDLLA FGKKKNLIVL DFQPLFRDKA YLARYIEPMR 

       130        140        150        160        170        180 
ILRERYGDVA QDVEMKFYDA NQYFSKYLLF ARTDAETVAG RVFTAYCDYL DLYWQLLASA 

       190        200        210        220        230        240 
APLGDAQDIR RIVKAQKDYD QYSADRDPAS GLFSSYFGHE WAERFLYEFL FEDAVPLAVG 


QPGR

Q7NL66 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools