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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541NADPBy similarity
Binding sitei117 – 1171FAD1 Publication
Binding sitei117 – 1171NADP; via amide nitrogenBy similarity
Binding sitei252 – 2521NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi51 – 544FAD1 Publication
Nucleotide bindingi67 – 693FAD1 Publication
Nucleotide bindingi74 – 774FAD1 Publication
Nucleotide bindingi144 – 1452NADPBy similarity
Nucleotide bindingi181 – 1822NADPBy similarity
Nucleotide bindingi220 – 2212NADPBy similarity
Nucleotide bindingi254 – 2585FAD1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2086-MONOMER.

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

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 258257Ferredoxin--NADP reductasePRO_0000167639Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi322710.Avin_38470.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1613Combined sources
Beta strandi19 – 257Combined sources
Beta strandi37 – 448Combined sources
Beta strandi47 – 548Combined sources
Beta strandi61 – 699Combined sources
Helixi77 – 804Combined sources
Beta strandi88 – 936Combined sources
Helixi101 – 1033Combined sources
Beta strandi108 – 1158Combined sources
Helixi116 – 1194Combined sources
Helixi120 – 1256Combined sources
Helixi129 – 1346Combined sources
Beta strandi136 – 14611Combined sources
Helixi147 – 1493Combined sources
Helixi153 – 1575Combined sources
Helixi160 – 1623Combined sources
Turni164 – 1663Combined sources
Helixi167 – 1737Combined sources
Beta strandi174 – 18310Combined sources
Beta strandi186 – 1894Combined sources
Helixi191 – 1966Combined sources
Helixi199 – 2046Combined sources
Turni211 – 2133Combined sources
Beta strandi214 – 2207Combined sources
Helixi222 – 23413Combined sources
Beta strandi247 – 2559Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8PX-ray2.00A1-258[»]
ProteinModelPortaliQ44532.
SMRiQ44532. Positions 2-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44532.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 102101FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DP0. Bacteria.
COG1018. LUCA.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8PX-ray2.00A1-258[»]
ProteinModelPortaliQ44532.
SMRiQ44532. Positions 2-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_38470.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DP0. Bacteria.
COG1018. LUCA.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2086-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ44532.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
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...

Publicationsi

  1. "Azotobacter vinelandii NADPH:ferredoxin reductase cloning, sequencing, and overexpression."
    Isas J.M., Yannone S.M., Burgess B.K.
    J. Biol. Chem. 270:21258-21263(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
  2. "Purification and characterization of a NADP+/NADPH-specific flavoprotein that is overexpressed in FdI-strains of Azotobacter vinelandii."
    Isas J.M., Burgess B.K.
    J. Biol. Chem. 269:19404-19409(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
  3. "The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii."
    Prasad G.S., Kresge N., Muhlberg A.B., Shaw A., Jung Y.S., Burgess B.K., Stout C.D.
    Protein Sci. 7:2541-2549(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FAD.
    Strain: LM100.

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 11, 2015
This is version 82 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.