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Protein

Ferredoxin--NADP reductase

Gene

petH

Organism
Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
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 sitei217NADPBy similarity1
Binding sitei237NADP1
Binding sitei241FAD1
Binding sitei294FAD1
Binding sitei294NADP; via amide nitrogen1
Binding sitei438NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 217FAD4
Nucleotide bindingi235 – 237FAD3
Nucleotide bindingi253 – 255FAD3
Nucleotide bindingi330 – 331NADPBy similarity2
Nucleotide bindingi360 – 361NADP2
Nucleotide bindingi370 – 374NADP5
Nucleotide bindingi399 – 400NADPBy similarity2

GO - Molecular functioni

  • ferredoxin-NADP+ reductase activity Source: UniProtKB
  • flavin adenine dinucleotide binding Source: UniProtKB
  • NADP binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.18.1.2. 319.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Phycobilisome, Thylakoid

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001676321 – 440Ferredoxin--NADP reductaseAdd BLAST440

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

IntActiP21890. 3 interactors.

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi144 – 147Combined sources4
Beta strandi151 – 153Combined sources3
Beta strandi158 – 167Combined sources10
Beta strandi173 – 175Combined sources3
Beta strandi177 – 183Combined sources7
Turni185 – 187Combined sources3
Beta strandi196 – 200Combined sources5
Beta strandi202 – 204Combined sources3
Beta strandi208 – 210Combined sources3
Beta strandi214 – 218Combined sources5
Turni222 – 227Combined sources6
Beta strandi228 – 237Combined sources10
Beta strandi240 – 242Combined sources3
Beta strandi243 – 248Combined sources6
Beta strandi249 – 251Combined sources3
Helixi253 – 259Combined sources7
Beta strandi266 – 273Combined sources8
Beta strandi275 – 277Combined sources3
Beta strandi286 – 292Combined sources7
Helixi293 – 295Combined sources3
Helixi296 – 307Combined sources12
Helixi309 – 314Combined sources6
Beta strandi324 – 332Combined sources9
Helixi333 – 335Combined sources3
Helixi339 – 348Combined sources10
Turni350 – 352Combined sources3
Beta strandi353 – 359Combined sources7
Turni360 – 362Combined sources3
Beta strandi368 – 370Combined sources3
Helixi373 – 379Combined sources7
Helixi381 – 388Combined sources8
Beta strandi393 – 399Combined sources7
Helixi403 – 416Combined sources14
Turni417 – 419Combined sources3
Helixi422 – 431Combined sources10
Beta strandi435 – 439Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21890.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 75CpcD-likePROSITE-ProRule annotationAdd BLAST59
Domaini155 – 279FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST125

Sequence similaritiesi

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

Family and domain databases

InterProiIPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF01383. CpcD. 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

« Hide

        10         20         30         40         50
MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV
60 70 80 90 100
PYNRMNQEMQ RITRLGGKIV TIQTVSALQQ LNGRTTIATV TDASSEIAKS
110 120 130 140 150
EGNGKATPVK TDSGAKAFAK PPAEEQLKKK DNKGNTMTQA KAKHADVPVN
160 170 180 190 200
LYRPNAPFIG KVISNEPLVK EGGIGIVQHI KFDLTGGNLK YIEGQSIGII
210 220 230 240 250
PPGVDKNGKP EKLRLYSIAS TRHGDDVDDK TISLCVRQLE YKHPESGETV
260 270 280 290 300
YGVCSTYLTH IEPGSEVKIT GPVGKEMLLP DDPEANVIML ATGTGIAPMR
310 320 330 340 350
TYLWRMFKDA ERAANPEYQF KGFSWLVFGV PTTPNILYKE ELEEIQQKYP
360 370 380 390 400
DNFRLTYAIS REQKNPQGGR MYIQDRVAEH ADELWQLIKN QKTHTYICGL
410 420 430 440
RGMEEGIDAA LSAAAAKEGV TWSDYQKDLK KAGRWHVETY
Length:440
Mass (Da):48,865
Last modified:October 1, 1994 - v2
Checksum:i8E1F61D0F09338B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti180I → L AA sequence (PubMed:3124746).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72394 Genomic DNA. Translation: CAA51088.1.
X54039 Genomic DNA. Translation: CAA37973.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72394 Genomic DNA. Translation: CAA51088.1.
X54039 Genomic DNA. Translation: CAA37973.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21890. 3 interactors.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.18.1.2. 319.

Miscellaneous databases

EvolutionaryTraceiP21890.

Family and domain databases

InterProiIPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF01383. CpcD. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 128 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

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.