Reviewed, UniProtKB/Swiss-Prot Q09545 (DHSB_CAEEL)

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
Synonyms:	tag-55
ORF Names:	F42A8.2

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	298 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 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.
Sequence caution	The sequence BAA23717.1 differs from that shown. Reason: Frameshift at positions 4, 15 and 28.

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	body morphogenesis Inferred from mutant phenotype. Source: WormBase electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW embryonic development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase growth Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase positive regulation of growth rate Inferred from mutant phenotype. Source: WormBase transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
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 Potential
	Chain	? – 298		Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000010354
Regions
	Domain	59 – 147	89	2Fe-2S ferredoxin-type
	Domain	190 – 220	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	107	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	112	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	115	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	127	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	200	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	203	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	206	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	210	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	215	1	Ubiquinone; shared with DHSD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q09545-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 0FDD148A6C9AB824	FASTA	298	32,891
	10 20 30 40 50 60 MLARSARLLH SAELAANAIR AASGAPATAA AAEASFPSTD DVAAKTKKTG NRIKTFEIYR 70 80 90 100 110 120 FNPEAPGAKP TVQKFDVDLD QCGTMILDAL IKIKNEVDPT LTFRRSCREG ICGSCAMNIG 130 140 150 160 170 180 GQNTLACICK IDSDTSKSTK IYPLPHMFVV KDLVPDMNLF YAQYASIQPW IQKKTPLTLG 190 200 210 220 230 240 EKQMHQSVAE RDRLDGLYEC ILCACCSTSC PSYWWNADKY LGPAVLMQAY RWVIDSRDDY 250 260 270 280 290 ATERLHRMHD SFSAFKCHTI MNCTKTCPKH LNPAKAIGEI KSLLTGFTSK PAAEPSAF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Stage-specific isoforms of Ascaris suum complex. II: The fumarate reductase of the parasitic adult and the succinate dehydrogenase of free-living larvae share a common iron-sulfur subunit." Amino H., Wang H., Hirawake H., Saruta F., Mizuchi D., Mineki R., Shindo N., Murayama K., Takamiya S., Aoki T., Kojima S., Kita K. Mol. Biochem. Parasitol. 106:63-76(2000) [PubMed: 10743611] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB008569 mRNA. Translation: BAA23717.1. Frameshift. Z47809 Genomic DNA. Translation: CAA87780.1.
PIR	T22083. T37260.
RefSeq	NP_495992.1.
UniGene	Cel.19522
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P07014.
SMR	Q09545. Positions 51-287.
ModBase	Search...
Protein-protein interaction databases
STRING	Q09545.
Genome annotation databases
Ensembl	F42A8.2.1; F42A8.2.1; F42A8.2; Caenorhabditis elegans. [Genome view] F42A8.2.2; F42A8.2.2; F42A8.2; Caenorhabditis elegans. [Genome view]
GeneID	174482.
KEGG	cel:F42A8.2.
Organism-specific databases
CTD	174482.
WormBase	WBGene00006433. sdhb-1.
WormPep	F42A8.2. CE01579. [WorfDB]
Phylogenomic databases
OMA	ADSRDDN.
Enzyme and pathway databases
BRENDA	1.3.5.1. 672.
Gene expression databases
ArrayExpress	Q09545.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. 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.
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...
Other Resources
NextBio	884224.

Entry information

Entry name

DHSB_CAEEL

Accession

Primary (citable) accession number: Q09545
Secondary accession number(s): O44075

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project