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Q9UTJ7 (SDHA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=FP
Gene names
Name:sdh1
ORF Names:SPAC1556.02c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) By similarity.

Catalytic activity

Succinate + ubiquinone = fumarate + ubiquinol.

Cofactor

FAD By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 641Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000010341

Regions

Nucleotide binding61 – 666FAD By similarity
Nucleotide binding84 – 9916FAD By similarity
Nucleotide binding450 – 4512FAD By similarity

Sites

Active site3331Proton acceptor By similarity
Binding site2681FAD By similarity
Binding site2891Substrate By similarity
Binding site3011Substrate By similarity
Binding site4001Substrate By similarity
Binding site4341FAD By similarity
Binding site4451Substrate By similarity

Amino acid modifications

Modified residue921Tele-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict2141A → G in BAA13924. Ref.2
Sequence conflict2181I → L in BAA13924. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UTJ7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5E5FCD857C372199

FASTA64170,466
        10         20         30         40         50         60 
MLRFRKVAPS LKNGGNLKLF STSSTLKKIA SSQPLRAKQV STSESVKYPV IDHTYDAIVV 

        70         80         90        100        110        120 
GAGGAGLRAT FGLAEAGFNT ACITKLFPTR SHTVAAQGGI NAALGNMTKD DWRWHFYDTV 

       130        140        150        160        170        180 
KGSDWLGDQD AIHYMTKEAP KAVLELEHFG VPFSRTKEGK IYQRAFGGQS LEYGKGGQAY 

       190        200        210        220        230        240 
RCAAVADRTG HSILHTLYGQ SLKHNTNFFI EYFAMDLIME GGECRGVIAM NLEDGSIHRF 

       250        260        270        280        290        300 
RAHKTILATG GYGRAYFSCT SAHTCTGDGN AMVSRAGLPL QDLEFVQFHP TGIYGAGCLI 

       310        320        330        340        350        360 
TEGCRGEGGY LLNSKGERFM ERYAPTAKDL ASRDVVSRAM TVEIREGRGV GPEKDHCYLQ 

       370        380        390        400        410        420 
LSHLPAEILK ERLPGISETA AIFAGVDVTK EPIPVLPTVH YNMGGIPTRF TGEVLTIDEN 

       430        440        450        460        470        480 
GKDKIVPGLY AAGEAACVSV HGGNRLGANS LLDIVVFGRA CALHIKDTLE PNTPHKPLAA 

       490        500        510        520        530        540 
DAGLDSLKFL DQIRTSQGPK HTSEIRLDMQ KTMQRDVSVF RMEETLQEGV KNIARVDGTY 

       550        560        570        580        590        600 
KDIGIRDRGL IWNTDLVEAL ELRNLLTCAV QTANAALNRK ESRGAHARED YPERDDKNWI 

       610        620        630        640 
KHTLTWQHKT GDPVTLKYRA VTRTTMDENE VKPVPPFKRV Y 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-641.
Strain: PR745.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB61213.1.
D89263 mRNA. Translation: BAA13924.1.
PIRT50081.
RefSeqNP_594319.1. NM_001019741.2.

3D structure databases

ProteinModelPortalQ9UTJ7.
SMRQ9UTJ7. Positions 47-641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278186. 4 interactions.
MINTMINT-4710641.
STRING4896.SPAC1556.02c-1.

Proteomic databases

PaxDbQ9UTJ7.
PRIDEQ9UTJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1556.02c.1; SPAC1556.02c.1:pep; SPAC1556.02c.
GeneID2541690.
KEGGspo:SPAC1556.02c.

Organism-specific databases

PomBaseSPAC1556.02c.

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
KOK00234.
OMAHGQVIIK.
OrthoDBEOG7V76G3.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802783.
PROQ9UTJ7.

Entry information

Entry nameSDHA_SCHPO
AccessionPrimary (citable) accession number: Q9UTJ7
Secondary accession number(s): P78912
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways