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Reviewed, UniProtKB/Swiss-Prot O13755 (FRDS_SCHPO)

Last modified November 3, 2009. Version 52. 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

Names and origin

Protein namesRecommended name:
    Putative fumarate reductase
Alternative name(s):
    NADH
    EC=1.3.1.6
    NADH-dependent fumarate reductase
    FAD-dependent oxidoreductase FRDS
Gene names
ORF Names: SPAC17A2.05
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Could be a fumarate reductase.

Catalytic activity

Succinate + NAD+ = fumarate + NADH.

Cofactor

FAD.

Subcellular location

Cytoplasm. Mitochondrion. Nucleus. Ref.2

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

mitochondrion Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

nucleus Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

fumarate reductase (NADH) activity

Inferred from electronic annotation. Source: EC

succinate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Putative fumarate reductase
PRO_0000316583

Regions

Nucleotide binding41 – 5515AMP Potential

Sites

Active site2881 By similarity
Active site3111 By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O13755-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9906AD63A570EC11

FASTA51355,484
        10         20         30         40         50         60 
MRCLTIYTWT FRRLPFIPST NSASFFSTLR FNMSTANNTQ AIVIGGGLAG LSATNTILDL 

        70         80         90        100        110        120 
GGNVLLLDKN TAFGGNSVKA ASGINAAPTQ LQFDQHVSDS VNTFYNDSIL SAKSKAKPEL 

       130        140        150        160        170        180 
LRTLTSKSSS AVDWLSERFG LQMDQLSRLA GHSEPRTHRG THPDYPFKPL AFVLVDQTEK 

       190        200        210        220        230        240 
FAASHPDRLQ IKKNARVTRL LTNPNHDKVF GVEYMDLSDK SNHTVYGPVV LATGGYAADY 

       250        260        270        280        290        300 
SDDSLLKLYH PEALSLSTTN GPYCTGDGHK MVMSIGGSTV DLDLVQIHPT GFVDPKDPTA 

       310        320        330        340        350        360 
LTKFLAAEAL RGSGAVLLTS QGRRFCDELG YRDYVTGEMM KLKSPVYLVL NSAAAEEVAN 

       370        380        390        400        410        420 
FIKFYSFKGL MKKMKAEELC STLNCTKDEL ASTFSEYNRA AKGEIPDEFG RKYFGKTPLE 

       430        440        450        460        470        480 
LTDTFTVGEV VPVLHYTMGG VQVDTQSRVL STNGNVIDGL FAAGEIVGGI HGENRLGGSS 

       490        500        510 
LLACVVFGRL AGQGASSTML RRFIASSTST ASS 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAB16560.1.
PIRT37806.
RefSeqNP_594239.1.

3D structure databases

HSSPHSSP built from PDB template 1D4D based on UniProtKB P83223.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13755.

Genome annotation databases

GeneID2542206.
KEGGspo:SPAC17A2.05.
NMPDRfig|4896.1.peg.4209.

Organism-specific databases

GeneDB_SpombeSPAC17A2.05.

Phylogenomic databases

OMAEWHCKHY.

Enzyme and pathway databases

BRENDA1.3.1.6. 653.

Gene expression databases

ArrayExpressO13755.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR010960. Flavocytochrome_c.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01813. flavo_cyto_c. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFRDS_SCHPO
AccessionPrimary (citable) accession number: O13755
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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