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=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(2003).

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

AF352050; AAK38599.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX548174; CAE19206.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_892865.1; -.

3D structure databases

ModBase

Q93TL5.

Enzyme and pathway databases

BioCyc

PMAR167540:PMM0747-MON; -.

Ontologies

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

Q93TL5.

Genome annotation databases

GeneID

1726068; -.

GenomeReviews

BX548174_GR; PMM0747.

KEGG

pmm:PMM0747; -.

NMPDR

fig|59919.1.peg.744; -.

Phylogenomic databases

HOGENOM

Q93TL5; -.

Genome annotation databases

CMR

Q93TL5; PMM0747.

Other

ProtoNet

Q93TL5.

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`	`1 241`	`241`		`Phycocyanobilin:ferredoxin oxidoreductase.`	`PRO_0000216743`

Sequence information

Length: 241 AA [This is the length of the unprocessed precursor]

Molecular weight: 28077 Da [This is the MW of the unprocessed precursor]

CRC64: B19E93EB85A45E68 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSKSLTKTK LIDPLILTLL QNIKVQRSKL NDLNCIEVDP KLSNIISNEE GKELYIENEF 

        70         80         90        100        110        120 
YKAKGFRKLH IEVAEFSKSL KILHCVFFPD PKYDIPIFGM DLVKVNELVS AAIVDLSPSS 

       130        140        150        160        170        180 
KNQNLKYDHL LSHIDKSVFK SKREIPIWGN IFSKNVFFAS LKNESEKNAF CKIVDNYLSV 

       190        200        210        220        230        240 
LIQLSQSTSP DSDYEIIEER INYQKNYCVQ QMKNEKTSLV LLKYFDKVWV DEYIKKVLFD 


F

Q93TL5 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