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Protein

Ferredoxin--NADP reductase

Gene

fpr

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54NADPBy similarity1
Binding sitei117FAD1 Publication1
Binding sitei117NADP; via amide nitrogenBy similarity1
Binding sitei252NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi51 – 54FAD1 Publication4
Nucleotide bindingi67 – 69FAD1 Publication3
Nucleotide bindingi74 – 77FAD1 Publication4
Nucleotide bindingi144 – 145NADPBy similarity2
Nucleotide bindingi181 – 182NADPBy similarity2
Nucleotide bindingi220 – 221NADPBy similarity2
Nucleotide bindingi254 – 258FAD1 Publication5

GO - Molecular functioni

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
Short name:
Protein X
Gene namesi
Name:fpr
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001676392 – 258Ferredoxin--NADP reductaseAdd BLAST257

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi322710.Avin_38470.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 16Combined sources13
Beta strandi19 – 25Combined sources7
Beta strandi37 – 44Combined sources8
Beta strandi47 – 54Combined sources8
Beta strandi61 – 69Combined sources9
Helixi77 – 80Combined sources4
Beta strandi88 – 93Combined sources6
Helixi101 – 103Combined sources3
Beta strandi108 – 115Combined sources8
Helixi116 – 119Combined sources4
Helixi120 – 125Combined sources6
Helixi129 – 134Combined sources6
Beta strandi136 – 146Combined sources11
Helixi147 – 149Combined sources3
Helixi153 – 157Combined sources5
Helixi160 – 162Combined sources3
Turni164 – 166Combined sources3
Helixi167 – 173Combined sources7
Beta strandi174 – 183Combined sources10
Beta strandi186 – 189Combined sources4
Helixi191 – 196Combined sources6
Helixi199 – 204Combined sources6
Turni211 – 213Combined sources3
Beta strandi214 – 220Combined sources7
Helixi222 – 234Combined sources13
Beta strandi247 – 255Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A8PX-ray2.00A1-258[»]
ProteinModelPortaliQ44532.
SMRiQ44532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44532.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 102FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST101

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105DP0. Bacteria.
COG1018. LUCA.

Family and domain databases

CDDicd06195. FNR1. 1 hit.
InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR033892. FNR_bac.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q44532-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNLNVERVL SVHHWNDTLF SFKTTRNPSL RFENGQFVMI GLEVDGRPLM
60 70 80 90 100
RAYSIASPNY EEHLEFFSIK VQNGPLTSRL QHLKEGDELM VSRKPTGTLV
110 120 130 140 150
TSDLLPGKHL YMLSTGTGLA PFMSLIQDPE VYERFEKVVL IHGVRQVNEL
160 170 180 190 200
AYQQFITEHL PQSEYFGEAV KEKLIYYPTV TRESFHNQGR LTDLMRSGKL
210 220 230 240 250
FEDIGLPPIN PQDDRAMICG SPSMLDESCE VLDGFGLKIS PRMGEPGDYL

IERAFVEK
Length:258
Mass (Da):29,417
Last modified:January 23, 2007 - v3
Checksum:i2865C2FC786A6C04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36319 Genomic DNA. Translation: AAA83029.1.
PIRiA57432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36319 Genomic DNA. Translation: AAA83029.1.
PIRiA57432.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A8PX-ray2.00A1-258[»]
ProteinModelPortaliQ44532.
SMRiQ44532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_38470.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DP0. Bacteria.
COG1018. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ44532.

Family and domain databases

CDDicd06195. FNR1. 1 hit.
InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR033892. FNR_bac.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFENR_AZOVI
AccessioniPrimary (citable) accession number: Q44532
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.