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Reviewed, UniProtKB/Swiss-Prot O31475 (FENR1_BACSU)

Last modified November 3, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1
      Short name=Fd-NADP+ reductase 1
      Short name=FNR 1
    EC=1.18.1.2
Gene names
Name: ycgT
Ordered Locus Names: BSU03270
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Homodimer By similarity.

Sequence similarities

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

Sequence caution

The sequence BAA08961.1 differs from that shown. Reason: Frameshift at positions 49 and 104.

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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 – 336336Ferredoxin--NADP reductase 1 HAMAP MF_01685
PRO_0000364801

Sites

Binding site371FAD By similarity
Binding site451FAD By similarity
Binding site501FAD By similarity
Binding site901FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1251FAD; via amide nitrogen By similarity
Binding site2871FAD By similarity
Binding site3281FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
O31475-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BF7F1617376AD742

FASTA33636,967
        10         20         30         40         50         60 
MAENQEVYDV TIIGGGPIGL FTAFYCGMRE LKTKVIEFLP KLGGKVSLFF PEKIIRDIGG 

        70         80         90        100        110        120 
IPGIAGKQLI EQLKEQAATF DPDIVLNQRV TGFERLDDGT IVLTGSEGKK HYTRTVILAC 

       130        140        150        160        170        180 
GMGTLEVNEF DSEDAARYAG KNLHYGVEKL DAFKGKRVVI SGGGDTAVDW ANELEPIAAS 

       190        200        210        220        230        240 
VTVVHRREEF GGMESSVTKM KQSSVRVLTP YRLEQLNGDE EGIKSVTVCH TESGQRKDIE 

       250        260        270        280        290        300 
IDELIINHGF KIDLGPMMEW GLEIEEGRVK ADRHMRTNLP GVFVAGDAAF YESKLRLIAG 

       310        320        330 
GFTEGPTAVN SAKAYLDPKA ENMAMYSTHH KKLVHK

« Hide

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References

« Hide 'large scale' references
[1]"The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
Yamane K., Kumano M., Kurita K.
Microbiology 142:3047-3056(1996) [PubMed: 8969502] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

D50453 Genomic DNA. Translation: BAA08961.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB12121.1.
PIRG69759.
RefSeqNP_388209.1.

3D structure databases

HSSPHSSP built from PDB template 1TRB based on UniProtKB P09625.
ModBaseSearch...

Proteomic databases

PRIDEO31475.

Genome annotation databases

GeneID938327.
GenomeReviewsGene locus BSU03270 in contig AL009126_GR.
KEGGbsu:BSU03270.
NMPDRfig|224308.1.peg.328.

Organism-specific databases

SubtiListBG12018. ycgT. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO31475.
OMAAYVSSHN.

Enzyme and pathway databases

BioCycBSUB224308:BSU0328-MON.

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...

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Entry information

Entry nameFENR1_BACSU
AccessionPrimary (citable) accession number: O31475
Secondary accession number(s): P94397
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 57 of the entry and version 1 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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