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P21911 (SDHB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 130. 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:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Iron-sulfur subunit of complex II
Short name=Ip
Gene names
Name:sdh2
ORF Names:SPAC140.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Iron-sulfur protein (IP) 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

Binds 1 2Fe-2S cluster By similarity.

Binds 1 3Fe-4S cluster By similarity.

Binds 1 4Fe-4S cluster 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 succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Potential
Chain25 – 275251Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
PRO_0000010350

Regions

Domain57 – 137812Fe-2S ferredoxin-type
Domain178 – 208314Fe-4S ferredoxin-type

Sites

Metal binding981Iron-sulfur (2Fe-2S) By similarity
Metal binding1031Iron-sulfur (2Fe-2S) By similarity
Metal binding1061Iron-sulfur (2Fe-2S) By similarity
Metal binding1181Iron-sulfur (2Fe-2S) By similarity
Metal binding1881Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1911Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1941Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1981Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2451Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2511Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2551Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2031Ubiquinone; shared with DHSD By similarity

Sequences

Sequence LengthMass (Da)Tools
P21911 [UniParc].

Last modified June 13, 2012. Version 3.
Checksum: F44661005266A678

FASTA27531,426
        10         20         30         40         50         60 
MFSRRIQVLS PFLKHFVNRN ARMMATEANI SATSANPQSQ GENLKTFEIY RWNPEKPEVK 

        70         80         90        100        110        120 
PKLQKYTVDL TKCGPMVLDA LIKIKNEQDP TLTFRRSCRE GICGSCAMNI NGSNTLACIC 

       130        140        150        160        170        180 
NIKKDNKPTK IYPLPHCFIV KDLVPDLTYF YKQYKSIEPW LQNDNIPKDK EFYQSRADRA 

       190        200        210        220        230        240 
KLDGLYECIL CACCSTSCPS YWWNSEEYLG PAVLMQAYRW IIDSRDQATA KRLDVMQNSM 

       250        260        270 
SVYRCHTIMN CARTCPKGLN PGLAIAKVKA LMATA 

« Hide

References

« Hide 'large scale' 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]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
[3]"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species."
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-251.
[4]Erratum
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB86412.2.
PIRD32394.
T37633.
RefSeqNP_593530.2. NM_001018964.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279288. 2 interactions.
MINTMINT-4687642.
STRING4896.SPAC140.01-1.

Proteomic databases

PaxDbP21911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC140.01.1; SPAC140.01.1:pep; SPAC140.01.
GeneID2542842.
KEGGspo:SPAC140.01.

Organism-specific databases

PomBaseSPAC140.01.

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
KOK00235.
OrthoDBEOG7X9GJ0.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803883.
PROP21911.

Entry information

Entry nameSDHB_SCHPO
AccessionPrimary (citable) accession number: P21911
Secondary accession number(s): P21915
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 13, 2012
Last modified: March 19, 2014
This is version 130 of the entry and version 3 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