Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ferredoxin--NADP reductase

Gene

CT1512

Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciCTEP194439:G1FZE-1551-MONOMER

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
OrganismiChlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
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

ProteinModelPortaliQ8KCB2
SMRiQ8KCB2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CAY Bacteria
COG0492 LUCA
HOGENOMiHOG000072909
KOiK00384
OMAiAFQCGMN
OrthoDBiPOG091H07EY

Family and domain databases

Gene3Di3.50.50.60, 3 hits
HAMAPiMF_01685 FENR2, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR022890 Fd--NADP_Rdtase_type_2
IPR000103 Pyridine_nuc-diS_OxRdtase_2
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
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
PATRICifig|194439.7.peg.1372

Similar proteinsi

Entry informationi

Entry nameiFENR_CHLTE
AccessioniPrimary (citable) accession number: Q8KCB2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 1, 2002
Last modified: March 28, 2018
This is version 94 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health