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Q8KCB2 (FENR_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase
Short name=FNR
Short name=Fd-NADP+ reductase
EC=1.18.1.2
Gene names
Ordered Locus Names:CT1512
OrganismChlorobium tepidum
Taxonomic identifier1097 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Ferredoxin--NADP reductase HAMAP MF_01685
PRO_0000364821

Sites

Binding site251FAD By similarity
Binding site441FAD By similarity
Binding site521FAD By similarity
Binding site571FAD By similarity
Binding site971FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1321FAD; via amide nitrogen By similarity
Binding site2981FAD By similarity
Binding site3391FAD By similarity

Secondary structure

1 ....................................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8KCB2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F016A6B0602475B1

FASTA36039,240
        10         20         30         40         50         60 
MLDIHNPATD HHDMRDLTII GGGPTGIFAA FQCGMNNISC RIIESMPQLG GQLAALYPEK 

        70         80         90        100        110        120 
HIYDVAGFPE VPAIDLVESL WAQAERYNPD VVLNETVTKY TKLDDGTFET RTNTGNVYRS 

       130        140        150        160        170        180 
RAVLIAAGLG AFEPRKLPQL GNIDHLTGSS VYYAVKSVED FKGKRVVIVG GGDSALDWTV 

       190        200        210        220        230        240 
GLIKNAASVT LVHRGHEFQG HGKTAHEVER ARANGTIDVY LETEVASIEE SNGVLTRVHL 

       250        260        270        280        290        300 
RSSDGSKWTV EADRLLILIG FKSNLGPLAR WDLELYENAL VVDSHMKTSV DGLYAAGDIA 

       310        320        330        340        350        360 
YYPGKLKIIQ TGLSEATMAV RHSLSYIKPG EKIRNVFSSV KMAKEKKAAE AGNATENKAE

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium."
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. expand/collapse author list , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49652 / DSM 12025 / TLS.
[2]"Purification and characterization of ferredoxin-NAD(P)(+) reductase from the green sulfur bacterium Chlorobium tepidum."
Seo D., Sakurai H.
Biochim. Biophys. Acta 1597:123-132(2002) [PubMed: 12009411] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006470 Genomic DNA. Translation: AAM72739.1.
RefSeqNP_662397.1. NC_002932.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AB1X-ray2.39A/B1-360[»]
ProteinModelPortalQ8KCB2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1006048.
GenomeReviewsGene locus CT1512 in contig AE006470_GR.
KEGGcte:CT1512.
NMPDRfig|194439.1.peg.1491.
PATRIC21400935. VBIChlTep116050_1372.
TIGRCT1512.

Phylogenomic databases

HOGENOMHBG669726.
OMAYPNKQKL.
ProtClustDBCLSK637801.

Enzyme and pathway databases

BioCycCTEP194439:CT_1512-MONOMER.

Family and domain databases

HAMAPMF_01685. FENR2.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR022890. Fd--NADP_Rdtase_type_2.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
KOK00384.
PANTHERPTHR22912:SF53. PTHR22912:SF53. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProtoNetSearch...

Entry information

Entry nameFENR_CHLTE
AccessionPrimary (citable) accession number: Q8KCB2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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