Q55CC2 (DHSB_DICDI) 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:	sdhB
ORF Names:	DDB_G0270120

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › 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; fumarate from succinate (eukaryal route): step 1/1.
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 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: dictyBase tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: dictyBase
Cellular_component	mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 3 iron, 4 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 4 iron, 4 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 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 electronic annotation. Source: EC ubiquinone binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion Potential
	Chain	24 – 287	264	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000327719
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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000005 Genomic DNA. Translation: EAL72410.1.
RefSeq	XP_646559.1. XM_641467.1.
3D structure databases
HSSP	HSSP built from PDB template 1YQ3 based on UniProtKB Q9YHT2.
ProteinModelPortal	Q55CC2.
SMR	Q55CC2. Positions 51-285.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0231383.
Proteomic databases
PRIDE	Q55CC2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231383; DDB0231383; DDB_G0270120.
GeneID	8617527.
KEGG	ddi:DDB_G0270120.
Organism-specific databases
dictyBase	DDB_G0270120. sdhB.
Phylogenomic databases
eggNOG	COG0479.
KO	K00235.
OMA	NCSRTCP.
ProtClustDB	CLSZ2431440.
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. PF13183. Fer4_8. 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...

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:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)