P21911 (DHSB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial electron transport, succinate to ubiquinone Inferred from sequence or structural similarity. Source: PomBase succinate metabolic process Inferred from sequence or structural similarity. Source: PomBase tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: PomBase
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from sequence or structural similarity. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 24	24	Mitochondrion Potential
	Chain	25 – 275	251	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000010350
Regions
	Domain	57 – 137	81	2Fe-2S ferredoxin-type
	Domain	178 – 208	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	98	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	103	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	106	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	118	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	188	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	191	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	194	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	198	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	245	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	251	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	255	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	203	1	Ubiquinone; shared with DHSD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21911 [UniParc]. Last modified June 13, 2012. Version 3. Checksum: F44661005266A678	FASTA	275	31,426
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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)

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB86412.2.
PIR	D32394. T37633.
RefSeq	NP_593530.2. NM_001018964.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC140.01-1.
Proteomic databases
PaxDb	P21911.
PRIDE	P21911.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC140.01.1; SPAC140.01.1:pep; SPAC140.01.
GeneID	2542842.
KEGG	spo:SPAC140.01.
Organism-specific databases
PomBase	SPAC140.01.
Phylogenomic databases
eggNOG	COG0479.
HOGENOM	HOG000160590.
KO	K00235.
OrthoDB	EOG4PRX0W.
Enzyme and pathway databases
UniPathway	UPA00223; UER01006.
Family and domain databases
Gene3D	1.10.1060.10. 1 hit. 3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. Beta-grasp_dom. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR004489. Succ_DH/fum_Rdtase_Fe-S. IPR025192. Succ_DH/fum_Rdtase_N. [Graphical view]
Pfam	PF13085. Fer2_3. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF46548. Helical_ferredxn. 1 hit.
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	PS00197. 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]
ProtoNet	Search...
Other
NextBio	20803883.

Entry information

Entry name

DHSB_SCHPO

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program