Reviewed, UniProtKB/Swiss-Prot P21911 (DHSB_SCHPO)

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 (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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.
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 sideBy 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
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 252		Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000010350
Regions
	Domain	34 – 114	81	2Fe-2S ferredoxin-type
	Domain	155 – 185	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	75	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	80	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	83	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	95	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	165	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	168	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	171	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	175	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	222	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	228	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	232	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	180	1	Ubiquinone; shared with DHSD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21911-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 87A3DC0B3742DEE1	FASTA	252	28,595
	10 20 30 40 50 60 MATEANISAT SANPQSQGEN LKTFEIYRWN PEKPEVKPKL QKYTVDLTKC GPMVLDALIK 70 80 90 100 110 120 IKNEQDPTLT FRRSCREGIC GSCAMNINGS NTLACICNIK KDNKPTKIYP LPHCFIVKDL 130 140 150 160 170 180 VPDLTYFYKQ YKSIEPWLQN DNIPKDKEFY QSRADRAKLD GLYECILCAC CSTSCPSYWW 190 200 210 220 230 240 NSEEYLGPAV LMQAYRWIID SRDQATAKRL DVMQNSMSVY RCHTIMNCAR TCPKGLNPGL 250 AIAKVKALMA TA

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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"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: 2494655] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-228.
[3]	Erratum Gould S.J., Subramani S., Scheffler I.E. Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB86412.1.
PIR	D32394. T37633.
RefSeq	NP_593530.1.
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P07014.
SMR	P21911. Positions 21-251.
ModBase	Search...
Genome annotation databases
GeneID	2542842.
KEGG	spo:SPAC140.01.
NMPDR	fig|4896.1.peg.3500.
Organism-specific databases
GeneDB_Spombe	SPAC140.01.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001211-MON.
Gene expression databases
ArrayExpress	P21911.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001450. 4Fe4S_Fe_S_bd. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DHase/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
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...

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:	December 15, 1998
Last modified:	November 25, 2008
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)