A8WPF0 (DHSB_CAEBR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 40.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Organism | Caenorhabditis briggsae [Reference proteome] | ||||
| Taxonomic identifier | 6238 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › 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 | |
| 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
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
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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. Waterston R.H.PLoS Biol. 1:166-192(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | HE600951 Genomic DNA. Translation: CAP22357.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 6238.CBG00872. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | CBG00872; CBG00872; CBG00872. |
Organism-specific databases | |
| WormBase | CBG00872; CBP34424; WBGene00024197; Cbr-sdhb-1. |
Phylogenomic databases | |
| eggNOG | COG0479. |
| HOGENOM | HOG000160590. |
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. [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_CAEBR | ||||||||
| Accession | Primary (citable) accession number: A8WPF0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
