Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A9NFF6 (FENR_ACHLI)

Last modified June 16, 2009. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Ferredoxin--NADP reductase
      Short name=Fd-NADP+ reductase
      Short name=FNR
    EC=1.18.1.2
Gene names
Ordered Locus Names: ACL_0467
OrganismAcholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]
Taxonomic identifier441768 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Hide | Top

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

General annotation (Comments)

Catalytic activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. HAMAP MF_01685

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

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

Hide | Top

Ontologies

Keywords
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

Inferred from electronic annotation. Source: HAMAP

NADP or NADPH binding

Inferred from electronic annotation. Source: HAMAP

ferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Ferredoxin--NADP reductase HAMAP MF_01685
PRO_0000364777

Sites

Binding site121FAD By similarity
Binding site311FAD By similarity
Binding site391FAD By similarity
Binding site441FAD By similarity
Binding site861FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1191FAD; via amide nitrogen By similarity
Binding site3171FAD By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A9NFF6-1 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 19D1821609F9E7CF

FASTA32236,026
        10         20         30         40         50         60 
MLEVLIIGAG PTGLYAAFLA GLRNLKAAVI ESSAEPGGQL TAVYKDKYIY DIPGFPKITA 

        70         80         90        100        110        120 
KDYIDGQVLQ YERFKSDLPI YYNEEAIDIK KHDDHFIVTT TTKTIETKFV LIAHGGGGFV 

       130        140        150        160        170        180 
PQKLKIDEHY DNILYFIKDL NQFKDKKIVV LGGGDSALDW AIDLSEYTKD VTLVHRRDEF 

       190        200        210        220        230        240 
RALQSSVDHF REKGTILTPY IVDTVEGNDK LVHTLVLKHA KTHERLNLDA DYIVVNYGFV 

       250        260        270        280        290        300 
LTKSRLDEWG IEGEKGLIKV DYTMKTSLDG IYAAGNGIDY PGKVKLISTG QGEAATAIQS 

       310        320 
ITTLLYPEKT RKFEHSTALI KE

« Hide

Hide | Top

References

[1]"Acholeplasma laidlawii complete genome."
Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.A., Kostrjukova E.S., Selezneva O.V., Vtyurin N.N., Rogov S.I., Alekseev D.G., Ladygina V.G. expand/collapse author list , Titova G.A., Karpov V.A., Govorun V.M.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CP000896 Genomic DNA. Translation: ABX81086.1. Different initiation.
RefSeqYP_001620462.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5803142.
GenomeReviewsGene locus ACL_0467 in contig CP000896_GR.
KEGGacl:ACL_0467.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01685.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameFENR_ACHLI
AccessionPrimary (citable) accession number: A9NFF6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 3, 2009
Last modified: June 16, 2009
This is version 15 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents