A8WPF0 (DHSB_CAEBR) 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-1
ORF Names:	CBG00872

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	282 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. UniProtKB Q9YHT2
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	Binds 1 2Fe-2S cluster By similarity. UniProtKB Q9YHT2 Binds 1 3Fe-4S cluster By similarity. UniProtKB Q9YHT2 Binds 1 4Fe-4S cluster By similarity. UniProtKB Q9YHT2
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. UniProtKB Q9YHT2
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity UniProtKB Q9YHT2.
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	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: UniProtKB-KW
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 – ?		Mitochondrion Potential
	Chain	? – 282		Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000367044
Regions
	Domain	43 – 131	89	2Fe-2S ferredoxin-type
	Domain	174 – 204	31	4Fe-4S ferredoxin-type
	Compositional bias	25 – 28	4	Poly-Ala
Sites
	Metal binding	91	1	Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q9YHT2
	Metal binding	96	1	Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q9YHT2
	Metal binding	99	1	Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q9YHT2
	Metal binding	111	1	Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q9YHT2
	Metal binding	184	1	Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q9YHT2
	Metal binding	187	1	Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q9YHT2
	Metal binding	190	1	Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q9YHT2
	Metal binding	194	1	Iron-sulfur 3 (3Fe-4S) By similarity UniProtKB Q9YHT2
	Metal binding	241	1	Iron-sulfur 3 (3Fe-4S) By similarity UniProtKB Q9YHT2
	Metal binding	247	1	Iron-sulfur 3 (3Fe-4S) By similarity UniProtKB Q9YHT2
	Metal binding	251	1	Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q9YHT2
	Binding site	199	1	Ubiquinone; shared with DHSD By similarity UniProtKB Q9YHT2

Sequences

	Sequence		Length	Mass (Da)
	A8WPF0 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 9A82F1BE0D05E8A1	FASTA	282	31,343
	10 20 30 40 50 60 MLARSALFVH SAELAANAAR AASGAAAAQP KKTGNRIKTF EIYRFNPEAP GAKPTIQKFD 70 80 90 100 110 120 VDLDQCGTMI LDALIKIKNE VDPTLTFRRS CREGICGSCA MNIGGENTLA CICKIDADTS 130 140 150 160 170 180 KSTKIYPLPH MFVVKDLVPD MNLFYAQYAS IQPWIQKKTP LTLGEKQMHQ SVAERDRLDG 190 200 210 220 230 240 LYECILCACC STSCPSYWWN ADKYLGPAVL MQAYRWVIDS RDDYAQERLH RMHDSFSAFK 250 260 270 280 CHTIMNCTKT CPKHLNPAKA IGEIKSLLTG FKSKPAAEPS AF

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000444 Genomic DNA. Translation: CAP22357.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8WPF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
WormBase	CBG00872; CBP34424; WBGene00024197.
Phylogenomic databases
HOGENOM	HBG616382.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR004489. Succ_DH/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.
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_CAEBR

Accession

Primary (citable) accession number: A8WPF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	December 16, 2008
Last modified:	September 21, 2011
This is version 30 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project