[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. DOI=10.1021/bi00127a009; PubMed=1554697 [NCBI, ExPASy, EBI, Israel, Japan] Schluchter W.M., Bryant D.A.; "Molecular characterization of ferredoxin-NADP+ oxidoreductase in cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies on the gene product."; Biochemistry 31:3092-3102(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.; "Complete sequence of Synechococcus sp. PCC 7002."; Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18. PubMed=8501038 [NCBI, ExPASy, EBI, Israel, Japan] Schluchter W.M., Zhao J., Bryant D.A.; "Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant."; J. Bacteriol. 175:3343-3352(1993).

Comments

CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP⁺ + H⁺ = 2 oxidized ferredoxin + NADPH.
COFACTOR: FAD.
SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=May be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.
SIMILARITY: Belongs to the ferredoxin--NADP reductase family.
SIMILARITY: Contains 1 cpcD-like domain.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

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

M86234; AAA27323.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000951; ACA98857.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M99378; AAA27310.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001734113.1; -.

3D structure databases

PDB

2B5O; X-ray; 2.50 A; A/B=1-402.

[ExPASy / RCSB / EBI]

PDBsum

2B5O; -.

ModBase

P31973.

Ontologies

GO:0030089;	Cellular component: phycobilisome (inferred from electronic annotation from InterPro).
GO:0042651;	Cellular component: thylakoid membrane (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004324;	Molecular function: ferredoxin-NADP+ reductase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001709; FPN_cyt_redctse.
IPR012146; Frd-NADP+_RD.
IPR015701; FRD_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR008213; Phycobilisome_lnk_CpcD-like.
Graphical view of domain structure.

PANTHER

PTHR19384:SF1; FRD_Red; 1.

Pfam

PF01383; CpcD; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000361; Frd-NADP+_RD; 1.

PRINTS

PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P31973.

Genome annotation databases

GeneID

6056783; -.

GenomeReviews

CP000951_GR; SYNPCC7002_A0853.

KEGG

syp:SYNPCC7002_A0853; -.

CMR

P31973; SYNPCC7002_A0853.

Other

UniRef

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

Keywords

3D-structure; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Membrane; NADP; Oxidoreductase; Phycobilisome; Thylakoid.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 402`	`402`	`Ferredoxin--NADP reductase.`	`PRO_0000167637`
`DOMAIN`	`1 80`	`80`	`CpcD-like.`
`DOMAIN`	`120 245`	`126`	`FAD-binding FR-type.`
`NP_BIND`	`254 272`	`19`	`NADP (By similarity).`
`DISULFID`	`219 224`		`By similarity.`
`STRAND`	`119 121`	`3`
`STRAND`	`123 132`	`10`
`STRAND`	`142 148`	`7`
`STRAND`	`161 165`	`5`
`STRAND`	`167 170`	`4`
`TURN`	`171 173`	`3`
`STRAND`	`179 183`	`5`
`TURN`	`187 192`	`6`
`STRAND`	`196 202`	`7`
`STRAND`	`205 207`	`3`
`TURN`	`209 211`	`3`
`STRAND`	`214 216`	`3`
`HELIX`	`218 224`	`7`
`STRAND`	`233 239`	`7`
`STRAND`	`252 258`	`7`
`HELIX`	`259 262`	`4`
`HELIX`	`263 273`	`11`
`STRAND`	`284 294`	`11`
`HELIX`	`295 297`	`3`
`HELIX`	`301 310`	`10`
`TURN`	`312 314`	`3`
`STRAND`	`315 321`	`7`
`TURN`	`322 324`	`3`
`HELIX`	`335 341`	`7`
`HELIX`	`343 350`	`8`
`STRAND`	`355 361`	`7`
`HELIX`	`363 365`	`3`
`HELIX`	`366 379`	`14`
`HELIX`	`384 393`	`10`
`STRAND`	`397 401`	`5`

Sequence information

Length: 402 AA [This is the length of the unprocessed precursor]

Molecular weight: 45015 Da [This is the MW of the unprocessed precursor]

CRC64: 5203060291BAFAE7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYGITSTANS TGNQSYANRL FIYEVVGLGG DGRNENSLVR KSGTTFITVP YARMNQEMQR 

        70         80         90        100        110        120 
ITKLGGKIVS IRPAEDAAQI VSEGQSSAQA SAQSPMASST KIVHPKTTDT SVPVNIYRPK 

       130        140        150        160        170        180 
TPFLGKCIEN YELVDEGGSG TVRHVTFDIS EGDLRYLEGQ SIGIIPPGED KNGKPHKLRL 

       190        200        210        220        230        240 
YSIASTRHGD MEDNKTVSLC VRQLEYQDPE SGETVYGVCS TYLCNLPVGT DDVKITGPVG 

       250        260        270        280        290        300 
KEMLLPDDED ATVVMLATGT GIAPFRAFLW RMFKEQHEDY KFKGKAWLIF GVPYTANILY 

       310        320        330        340        350        360 
KDDFEKMAAE NPDNFRLTYA ISREQKTADG GKVYVQSRVS EYADELFEMI QKPNTHVYMC 

       370        380        390        400 
GLKGMQPPID ETFTAEAEKR GLNWEEMRRS MKKEHRWHVE VY

P31973 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