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P21890

- FENR_NOSSO

UniProt

P21890 - FENR_NOSSO

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Protein

Ferredoxin--NADP reductase

Gene
petH
Organism
Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei217 – 2171NADP By similarity
Binding sitei237 – 2371NADP
Binding sitei241 – 2411FAD
Binding sitei294 – 2941FAD
Binding sitei294 – 2941NADP; via amide nitrogen
Binding sitei438 – 4381NADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2174FAD
Nucleotide bindingi235 – 2373FAD
Nucleotide bindingi253 – 2553FAD
Nucleotide bindingi330 – 3312NADP By similarity
Nucleotide bindingi360 – 3612NADP
Nucleotide bindingi370 – 3745NADP
Nucleotide bindingi399 – 4002NADP By similarity

GO - Molecular functioni

  1. ferredoxin-NADP+ reductase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: UniProtKB
  3. NADP binding Source: UniProtKB
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin--NADP reductase (EC:1.18.1.2)
Short name:
FNR
Gene namesi
Name:petH
OrganismiNostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
Taxonomic identifieri1168 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Subcellular locationi

Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side
Note: May be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.

GO - Cellular componenti

  1. phycobilisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Phycobilisome, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Ferredoxin--NADP reductasePRO_0000167632Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
isiBP0A3E05EBI-593915,EBI-593907
petFP0A3C85EBI-593915,EBI-637080

Protein-protein interaction databases

IntActiP21890. 3 interactions.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi144 – 1474
Beta strandi151 – 1533
Beta strandi158 – 16710
Beta strandi173 – 1753
Beta strandi177 – 1837
Turni185 – 1873
Beta strandi196 – 2005
Beta strandi202 – 2043
Beta strandi208 – 2103
Beta strandi214 – 2185
Turni222 – 2276
Beta strandi228 – 23710
Beta strandi240 – 2423
Beta strandi243 – 2486
Beta strandi249 – 2513
Helixi253 – 2597
Beta strandi266 – 2738
Beta strandi275 – 2773
Beta strandi286 – 2927
Helixi293 – 2953
Helixi296 – 30712
Helixi309 – 3146
Beta strandi324 – 3329
Helixi333 – 3353
Helixi339 – 34810
Turni350 – 3523
Beta strandi353 – 3597
Turni360 – 3623
Beta strandi368 – 3703
Helixi373 – 3797
Helixi381 – 3888
Beta strandi393 – 3997
Helixi403 – 41614
Turni417 – 4193
Helixi422 – 43110
Beta strandi435 – 4395

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B2RX-ray1.80A137-440[»]
1BJKX-ray2.30A146-440[»]
1BQEX-ray2.45A146-440[»]
1E62X-ray2.30A137-440[»]
1E63X-ray2.30A137-440[»]
1E64X-ray2.30A137-440[»]
1EWYX-ray2.38A/B138-440[»]
1GJRX-ray2.10A137-440[»]
1GO2X-ray1.70A137-440[»]
1GR1X-ray2.50A138-440[»]
1H42X-ray2.15A137-440[»]
1H85X-ray2.30A146-440[»]
1OGIX-ray1.64A138-440[»]
1OGJX-ray1.64A138-440[»]
1QGYX-ray1.70A146-440[»]
1QGZX-ray2.30A146-440[»]
1QH0X-ray1.93A146-440[»]
1QUEX-ray1.80A138-440[»]
1QUFX-ray2.25A137-440[»]
1W34X-ray1.73A137-440[»]
1W35X-ray1.90A137-440[»]
1W87X-ray3.00A/B137-440[»]
2BMWX-ray1.50A137-440[»]
2BSAX-ray1.92A138-440[»]
2VYQX-ray1.90A137-440[»]
2VZLX-ray1.93A137-440[»]
2X3UX-ray1.93A138-440[»]
3ZBTX-ray1.92A138-440[»]
3ZBUX-ray1.89A138-440[»]
3ZC3X-ray2.30A/B138-440[»]
4BPRX-ray2.00A138-440[»]
4C43X-ray1.70A138-440[»]
ProteinModelPortaliP21890.
SMRiP21890. Positions 138-440.

Miscellaneous databases

EvolutionaryTraceiP21890.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 7559CpcD-likeAdd
BLAST
Domaini155 – 279125FAD-binding FR-typeAdd
BLAST

Sequence similaritiesi

Contains 1 cpcD-like domain.

Family and domain databases

InterProiIPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF01383. CpcD. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSiPR00371. FPNCR.
SMARTiSM01094. CpcD. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51441. CPCD_LIKE. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21890-1 [UniParc]FASTAAdd to Basket

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MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV    50
PYNRMNQEMQ RITRLGGKIV TIQTVSALQQ LNGRTTIATV TDASSEIAKS 100
EGNGKATPVK TDSGAKAFAK PPAEEQLKKK DNKGNTMTQA KAKHADVPVN 150
LYRPNAPFIG KVISNEPLVK EGGIGIVQHI KFDLTGGNLK YIEGQSIGII 200
PPGVDKNGKP EKLRLYSIAS TRHGDDVDDK TISLCVRQLE YKHPESGETV 250
YGVCSTYLTH IEPGSEVKIT GPVGKEMLLP DDPEANVIML ATGTGIAPMR 300
TYLWRMFKDA ERAANPEYQF KGFSWLVFGV PTTPNILYKE ELEEIQQKYP 350
DNFRLTYAIS REQKNPQGGR MYIQDRVAEH ADELWQLIKN QKTHTYICGL 400
RGMEEGIDAA LSAAAAKEGV TWSDYQKDLK KAGRWHVETY 440
Length:440
Mass (Da):48,865
Last modified:October 1, 1994 - v2
Checksum:i8E1F61D0F09338B6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801I → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X72394 Genomic DNA. Translation: CAA51088.1.
X54039 Genomic DNA. Translation: CAA37973.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X72394 Genomic DNA. Translation: CAA51088.1 .
X54039 Genomic DNA. Translation: CAA37973.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B2R X-ray 1.80 A 137-440 [» ]
1BJK X-ray 2.30 A 146-440 [» ]
1BQE X-ray 2.45 A 146-440 [» ]
1E62 X-ray 2.30 A 137-440 [» ]
1E63 X-ray 2.30 A 137-440 [» ]
1E64 X-ray 2.30 A 137-440 [» ]
1EWY X-ray 2.38 A/B 138-440 [» ]
1GJR X-ray 2.10 A 137-440 [» ]
1GO2 X-ray 1.70 A 137-440 [» ]
1GR1 X-ray 2.50 A 138-440 [» ]
1H42 X-ray 2.15 A 137-440 [» ]
1H85 X-ray 2.30 A 146-440 [» ]
1OGI X-ray 1.64 A 138-440 [» ]
1OGJ X-ray 1.64 A 138-440 [» ]
1QGY X-ray 1.70 A 146-440 [» ]
1QGZ X-ray 2.30 A 146-440 [» ]
1QH0 X-ray 1.93 A 146-440 [» ]
1QUE X-ray 1.80 A 138-440 [» ]
1QUF X-ray 2.25 A 137-440 [» ]
1W34 X-ray 1.73 A 137-440 [» ]
1W35 X-ray 1.90 A 137-440 [» ]
1W87 X-ray 3.00 A/B 137-440 [» ]
2BMW X-ray 1.50 A 137-440 [» ]
2BSA X-ray 1.92 A 138-440 [» ]
2VYQ X-ray 1.90 A 137-440 [» ]
2VZL X-ray 1.93 A 137-440 [» ]
2X3U X-ray 1.93 A 138-440 [» ]
3ZBT X-ray 1.92 A 138-440 [» ]
3ZBU X-ray 1.89 A 138-440 [» ]
3ZC3 X-ray 2.30 A/B 138-440 [» ]
4BPR X-ray 2.00 A 138-440 [» ]
4C43 X-ray 1.70 A 138-440 [» ]
ProteinModelPortali P21890.
SMRi P21890. Positions 138-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21890. 3 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P21890.

Family and domain databases

InterProi IPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF01383. CpcD. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSi PR00371. FPNCR.
SMARTi SM01094. CpcD. 1 hit.
[Graphical view ]
SUPFAMi SSF63380. SSF63380. 1 hit.
PROSITEi PS51441. CPCD_LIKE. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Homology of the N-terminal domain of the petH gene product from Anabaena sp. PCC 7119 to the CpcD phycobilisome linker polypeptide."
    Fillat M.F., Flores E., Gomez-Moreno C.
    Plant Mol. Biol. 22:725-729(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of the ferredoxin-NADP(+)-reductase gene from Anabaena PCC 7119."
    Fillat M.F., Bakker H.A.C., Weisbeek P.J.
    Nucleic Acids Res. 18:7161-7161(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-440.
  3. "Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacteria Anabaena variabilis."
    Sancho J., Peleato M.L., Gomez-Moreno C., Edmondson D.E.
    Arch. Biochem. Biophys. 260:200-207(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 152-183.
    Strain: 1403.46.
  4. "X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8-A resolution, and crystallographic studies of NADP+ binding at 2.25-A resolution."
    Serre L., Vellieux F.M.D., Medina M., Gomez-Moreno C., Fontecilla-Camps J.-C., Frey M.
    J. Mol. Biol. 263:20-39(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
  5. "Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer."
    Martinez-Julvez M., Hermoso J., Hurley J.K., Mayoral T., Sanz-Aparicio J., Tollin G., Gomez-Moreno C., Medina M.
    Biochemistry 37:17680-17691(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-440.
  6. "Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by X-ray crystallography."
    Mayoral T., Medina M., Sanz-Aparicio J., Gomez-Moreno C., Hermoso J.A.
    Proteins 38:60-69(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
  7. "Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule."
    Morales R., Kachalova G., Vellieux F., Charon M.-H., Frey M.
    Acta Crystallogr. D 56:1408-1412(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).

Entry informationi

Entry nameiFENR_NOSSO
AccessioniPrimary (citable) accession number: P21890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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