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P00454 (FENR_SPISP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismSpirulina sp.
Taxonomic identifier1157 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Oscillatoriales › Spirulina

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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.

Sequence similarities

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

Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
   Cellular componentMembrane
Phycobilisome
Thylakoid
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentphycobilisome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

ferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Ferredoxin--NADP reductase
PRO_0000167635

Regions

Domain13 – 137125FAD-binding FR-type
Nucleotide binding72 – 754FAD By similarity
Nucleotide binding93 – 953FAD By similarity
Nucleotide binding111 – 1133FAD By similarity
Nucleotide binding184 – 1852NADP By similarity
Nucleotide binding214 – 2152NADP By similarity
Nucleotide binding224 – 2285NADP By similarity
Nucleotide binding253 – 2542NADP By similarity

Sites

Binding site751NADP By similarity
Binding site951NADP By similarity
Binding site991FAD By similarity
Binding site1521FAD By similarity
Binding site1521NADP; via amide nitrogen By similarity
Binding site2241NADP By similarity
Binding site2921NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P00454 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 8761AB97B04C8CD5

FASTA29433,349
        10         20         30         40         50         60 
AKTDIPVNIY KPKNPYIGKC LSNEELVREG GTGTVRHLIF DISGGDLRYL EGQSIGIIPP 

        70         80         90        100        110        120 
GTDNNGKPHK LRLYSIASTR HGDHVDDKTV SLCVRQLEYK HPETGETVYG VCSTYLCNLE 

       130        140        150        160        170        180 
AGADVAITGP VGKEMLLPED EDATIIMMAT GTGIAPFRAF LWRIFKEQHE DYKFKGLAWL 

       190        200        210        220        230        240 
FFGIPYSPNI LYQQELEELQ EEFPENFRLT LAISREQQNP EGGKMYIQDR IKENADQLWE 

       250        260        270        280        290 
LIQKPNTHTY ICGLKGMEGG IDEGMSAAAG KFDVDWSDYQ KELKKKHRWH VETY

« Hide

References

[1]"Spirulina ferredoxin-NADP+ reductase. The complete amino acid sequence."
Yao Y., Tamura T., Wada K., Matsubara H., Kodo K.
J. Biochem. 95:1513-1516(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, SEQUENCE REVISION.
[2]"Spirulina ferredoxin-NADP+ reductase. Further characterization with an improved preparation."
Wada K., Tamura T., Matsubara H., Kodo K.
J. Biochem. 94:387-393(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.

Cross-references

Sequence databases

PIRRDSGXX. A00531.

3D structure databases

ProteinModelPortalP00454.
SMRP00454. Positions 5-294.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR015701. Fd_Red.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. FNR.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR19384:SF1. PTHR19384:SF1. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFENR_SPISP
AccessionPrimary (citable) accession number: P00454
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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