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Reviewed, UniProtKB/Swiss-Prot Q5PAR7 (FENR_ANAMM)

Last modified January 19, 2010. Version 41. 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

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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: AM617
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

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Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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. HAMAP MF_01685

Subunit structure

Homodimer By similarity. HAMAP MF_01685

Sequence similarities

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

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Ferredoxin--NADP reductase HAMAP MF_01685
PRO_0000364782

Sites

Binding site281FAD By similarity
Binding site361FAD By similarity
Binding site411FAD By similarity
Binding site811FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1151FAD; via amide nitrogen By similarity
Binding site2821FAD By similarity
Binding site3231FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5PAR7-1 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 2DF62F042E704294

FASTA32935,705
        10         20         30         40         50         60 
MAIIGAGPVG LFTVFQAGML GMSACVIDAL SEVGGQCAVL YPEKPIYDIP AYPVTLARDL 

        70         80         90        100        110        120 
VNNLKRQADP FKPTYLLGHT AEQVLEEGEH FVVVTDKKVG VRCRAIVIAA GSGGFGPNRP 

       130        140        150        160        170        180 
PLDGITEYED KSVFYHVSDV SRFRGKRVVI AGGGDSAADW AVSLSEVADS VHVIHRRHSF 

       190        200        210        220        230        240 
RCAPNTLRNL ESLAERGQIK LLVPYQLAGL AGSDGMLNGV IIRNISSKEE TRIDADFLLP 

       250        260        270        280        290        300 
FFGISAKLGP IANWGLGVES FYIPIDQSTC RTARTRIYAV GDVAHYQGKL KLILVGFSES 

       310        320 
ALACHDIYKV LFPETPLNFQ YSTSKKMPC

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References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000030 Genomic DNA. Translation: AAV86613.1. Different initiation.
RefSeqYP_153868.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PAR7.

Genome annotation databases

GeneID3171421.
GenomeReviewsGene locus AM617 in contig CP000030_GR.
KEGGama:AM617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMAIYLVHRR.

Enzyme and pathway databases

BioCycAMAR234826:AM617-MONOMER.

Family and domain databases

HAMAPMF_01685. FENR2.
[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.
ProtoNetSearch...

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Entry information

Entry nameFENR_ANAMM
AccessionPrimary (citable) accession number: Q5PAR7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 3, 2009
Last modified: January 19, 2010
This is version 41 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)

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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