Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial precursor

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Q09545 (DHSB_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › 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; 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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
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

? – 298

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000010354

Regions

Domain

59 – 147

2Fe-2S ferredoxin-type

Domain

190 – 220

4Fe-4S ferredoxin-type

Sites

Metal binding

107

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

112

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

115

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

127

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

200

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

203

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

206

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

210

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

257

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

263

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

267

Iron-sulfur 2 (4Fe-4S) By similarity

Binding site

215

Ubiquinone; shared with DHSD By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q09545 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0FDD148A6C9AB824
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB008569 mRNA. Translation: BAA23717.1. Frameshift. Z47809 Genomic DNA. Translation: CAA87780.1.
PIR	T22083. T37260.
RefSeq	NP_495992.1. NM_063591.6.
3D structure databases
ProteinModelPortal	Q09545.
SMR	Q09545. Positions 52-296.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.F42A8.2.2.
Proteomic databases
PaxDb	Q09545.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F42A8.2.1; F42A8.2.1; F42A8.2. F42A8.2.2; F42A8.2.2; F42A8.2.
GeneID	174482.
KEGG	cel:CELE_F42A8.2.
Organism-specific databases
CTD	174482.
WormBase	F42A8.2; CE01579; WBGene00006433; sdhb-1.
Phylogenomic databases
eggNOG	COG0479.
GeneTree	ENSGT00390000013558.
HOGENOM	HOG000160590.
InParanoid	Q09545.
KO	K00235.
OMA	NCSRTCP.
Enzyme and pathway databases
UniPathway	UPA00223; UER01006.
Gene expression databases
ArrayExpress	Q09545.
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. [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...
Other
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:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents