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Protein

Ferredoxin--NADP reductase

Gene

CT1512

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.1 Publication

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei25FADBy similarity1
Binding sitei44FADBy similarity1
Binding sitei52FADBy similarity1
Binding sitei57FADBy similarity1
Binding sitei97FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei132FAD; via amide nitrogenBy similarity1
Binding sitei298FADBy similarity1
Binding sitei339FADBy similarity1

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:
Fd-NADP(+) reductase
Gene namesi
Ordered Locus Names:CT1512
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003648211 – 360Ferredoxin--NADP reductaseAdd BLAST360

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi194439.CT1512.

Structurei

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 20Combined sources6
Helixi24 – 35Combined sources12
Beta strandi40 – 43Combined sources4
Beta strandi45 – 49Combined sources5
Helixi51 – 55Combined sources5
Beta strandi60 – 62Combined sources3
Beta strandi69 – 72Combined sources4
Helixi73 – 85Combined sources13
Beta strandi90 – 92Combined sources3
Beta strandi97 – 102Combined sources6
Beta strandi108 – 112Combined sources5
Beta strandi117 – 125Combined sources9
Helixi138 – 140Combined sources3
Turni144 – 146Combined sources3
Turni148 – 150Combined sources3
Beta strandi151 – 154Combined sources4
Helixi158 – 161Combined sources4
Beta strandi165 – 169Combined sources5
Helixi173 – 181Combined sources9
Turni182 – 185Combined sources4
Beta strandi186 – 192Combined sources7
Beta strandi194 – 197Combined sources4
Helixi203 – 206Combined sources4
Helixi209 – 213Combined sources5
Beta strandi216 – 231Combined sources16
Beta strandi234 – 242Combined sources9
Beta strandi247 – 251Combined sources5
Beta strandi253 – 257Combined sources5
Helixi266 – 270Combined sources5
Beta strandi279 – 281Combined sources3
Beta strandi293 – 295Combined sources3
Helixi309 – 327Combined sources19
Helixi338 – 347Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AB1X-ray2.39A/B1-360[»]
ProteinModelPortaliQ8KCB2.
SMRiQ8KCB2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CAY. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072909.
KOiK00384.
OMAiLDYQTNI.
OrthoDBiPOG091H07EY.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_01685. FENR2. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR022890. Fd--NADP_Rdtase_type_2.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8KCB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDIHNPATD HHDMRDLTII GGGPTGIFAA FQCGMNNISC RIIESMPQLG
60 70 80 90 100
GQLAALYPEK HIYDVAGFPE VPAIDLVESL WAQAERYNPD VVLNETVTKY
110 120 130 140 150
TKLDDGTFET RTNTGNVYRS RAVLIAAGLG AFEPRKLPQL GNIDHLTGSS
160 170 180 190 200
VYYAVKSVED FKGKRVVIVG GGDSALDWTV GLIKNAASVT LVHRGHEFQG
210 220 230 240 250
HGKTAHEVER ARANGTIDVY LETEVASIEE SNGVLTRVHL RSSDGSKWTV
260 270 280 290 300
EADRLLILIG FKSNLGPLAR WDLELYENAL VVDSHMKTSV DGLYAAGDIA
310 320 330 340 350
YYPGKLKIIQ TGLSEATMAV RHSLSYIKPG EKIRNVFSSV KMAKEKKAAE
360
AGNATENKAE
Length:360
Mass (Da):39,240
Last modified:October 1, 2002 - v1
Checksum:iF016A6B0602475B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72739.1.
RefSeqiNP_662397.1. NC_002932.3.
WP_010933178.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM72739; AAM72739; CT1512.
GeneIDi1006048.
KEGGicte:CT1512.
PATRICi21400935. VBIChlTep116050_1372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72739.1.
RefSeqiNP_662397.1. NC_002932.3.
WP_010933178.1. NC_002932.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AB1X-ray2.39A/B1-360[»]
ProteinModelPortaliQ8KCB2.
SMRiQ8KCB2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi194439.CT1512.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM72739; AAM72739; CT1512.
GeneIDi1006048.
KEGGicte:CT1512.
PATRICi21400935. VBIChlTep116050_1372.

Phylogenomic databases

eggNOGiENOG4105CAY. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072909.
KOiK00384.
OMAiLDYQTNI.
OrthoDBiPOG091H07EY.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_01685. FENR2. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR022890. Fd--NADP_Rdtase_type_2.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFENR_CHLTE
AccessioniPrimary (citable) accession number: Q8KCB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.