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Q55318 (FENR_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase
Short name=FNR
EC=1.18.1.2
Gene names
Name:petH
Ordered Locus Names:slr1643
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for growth.

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.

Induction

By light, and also by 0.55 M NaCl. Ref.1

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Contains 1 cpcD-like domain.

Contains 1 FAD-binding FR-type domain.

Biophysicochemical properties

Kinetic parameters:

The enzyme was overproduced in E.coli.

KM=21 µM for NADPH (at 25 degrees Celsius) Ref.1

Vmax=110 µmol/min/mg enzyme toward NADPH (at 25 degrees Celsius)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Ferredoxin--NADP reductase
PRO_0000167638

Regions

Domain18 – 7659CpcD-like
Domain133 – 256124FAD-binding FR-type
Nucleotide binding192 – 1954FAD By similarity
Nucleotide binding213 – 2153FAD By similarity
Nucleotide binding230 – 2323FAD By similarity
Nucleotide binding303 – 3042NADP By similarity
Nucleotide binding333 – 3342NADP By similarity
Nucleotide binding343 – 3475NADP By similarity
Nucleotide binding372 – 3732NADP By similarity

Sites

Binding site1951NADP By similarity
Binding site2151NADP By similarity
Binding site2191FAD By similarity
Binding site2711FAD By similarity
Binding site2711NADP; via amide nitrogen By similarity
Binding site4111NADP By similarity

Experimental info

Sequence conflict1821E → K in CAA63961. Ref.1
Sequence conflict2431D → S in CAA63961. Ref.1
Sequence conflict347 – 3504QHRV → STGL in CAA63961. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q55318 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: FF33709639F0CAA8

FASTA41346,360
        10         20         30         40         50         60 
MYSPGYVATS SRQSDAGNRL FVYEVIGLSQ STMTDGLDYP IRRSGSTFIT VPLKRMNQEM 

        70         80         90        100        110        120 
RRITRMGGKI VSIKPLEGDS PLPHTEGIAK PSQSEGSGSE AVANPAPESN KTMTTTPKEK 

       130        140        150        160        170        180 
KADDIPVNIY RPKTPYIGKV LENYPLVREG AIGTVQHLTF DLSAGDLRYL EGQSIGIIPP 

       190        200        210        220        230        240 
GEDDKGKPHK LRLYSIASTR HGDFGDDKTV SLCVRQLEYQ NEAGETVQGV CSTYLCNIKE 

       250        260        270        280        290        300 
GDDIAITGPV GKEMLLPPDE DANIVMLATG TGIAPFRAFL WRMFKEQHED YKFKGLAWLI 

       310        320        330        340        350        360 
FGIPKSENIL YKDDLEKMAA EFPDNFRLTY AISREQQNAE GGRMYIQHRV AENAEELWNL 

       370        380        390        400        410 
MQNPKTHTYM CGLKGMEPGI DEAFTALAEQ NGKEWTTFQR EMKKEHRWHV ETY

« Hide

References

« Hide 'large scale' references
[1]"Characterization and transcriptional regulation of the Synechocystis PCC 6803 petH gene, encoding ferredoxin-NADP+ oxidoreductase: involvement of a novel type of divergent operator."
van Thor J.J., Hellingwerf K.J., Matthijs H.C.P.
Plant Mol. Biol. 36:353-363(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X94297 Genomic DNA. Translation: CAA63961.1.
BA000022 Genomic DNA. Translation: BAA18459.1.
PIRS76200.
RefSeqNP_441779.1. NC_000911.1.
YP_005651838.1. NC_017277.1.
YP_007451660.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55318.
SMRQ55318. Positions 125-413.
ModBaseSearch...

Protein-protein interaction databases

IntActQ55318. 1 interaction.
MINTMINT-1353922.
STRING1148.slr1643.

Proteomic databases

PaxDbQ55318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18459; BAA18459; BAA18459.
GeneID12254494.
14617324.
952929.
KEGGsyn:slr1643.
syy:SYNGTS_1885.
PATRIC23841044. VBISynSp132158_2075.

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000220125.
KOK02641.
OMAGRMYIQD.
ProtClustDBCLSK893276.

Enzyme and pathway databases

BRENDA1.18.1.2. 6185.

Family and domain databases

InterProIPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR015701. Fd_Red.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR19384:SF1. PTHR19384:SF1. 1 hit.
PfamPF01383. CpcD. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
SMARTSM01094. CpcD. 1 hit.
[Graphical view]
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51441. CPCD_LIKE. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFENR_SYNY3
AccessionPrimary (citable) accession number: Q55318
Secondary accession number(s): P74364
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

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