Reviewed, UniProtKB/Swiss-Prot Q55CC2 (DHSB_DICDI)

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(s)=Ip

Gene names

Name:	sdhB
ORF Names:	DDB_0231383

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	287 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.
Subunit structure	Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, 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)
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion Potential
	Chain	24 – 287	264	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Regions
	Domain	51 – 140	90	2Fe-2S ferredoxin-type
	Domain	186 – 216	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	101	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	106	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	109	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	121	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	196	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	199	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	202	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	206	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	257	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	263	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	267	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	211	1	Ubiquinone; shared with DHSD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55CC2-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 86BF6C9A4980D0C4	FASTA	287	32,185
	10 20 30 40 50 60 MISNVLKRAS VLARSNGIQS AFYTTTAKTE ASSSPQMKIK TAEKKDHFVN FQVYRYNEET 70 80 90 100 110 120 TAKPYIQTYN INLKDCGPMV LDALLLIKNN IDPTLSFRRS CREGICGSCA MNLNGSNTLA 130 140 150 160 170 180 CTKKITDCLS GDTVKVYPLP HMHVVRDLIP DLSHFYTQHK SIKPWLEPAV DVPRYNGKEI 190 200 210 220 230 240 LQSKENRHKL DGLYECILCA CCSTSCPSYW WSEGGDGGYL GPAVLLQAYR WIADSRDSIQ 250 260 270 280 KDRLAILSED QMKVYKCHTI MNCTAVCPKG LNPGKSIANI KYLLAHN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000005 Genomic DNA. Translation: EAL72410.1.
RefSeq	XP_646559.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3397440.
KEGG	ddi:DDB_0231383.
Organism-specific databases
dictyBase	DDB0231383. sdhB.
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]
ProDom	Q55CC2. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

DHSB_DICDI

Accession

Primary (citable) accession number: Q55CC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	July 22, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)