Reviewed,
UniProtKB/Swiss-Prot P80909 (VORC_METTM)
Last modified
November 4, 2008.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Ketoisovalerate oxidoreductase subunit vorC Short name=VOR EC=1.2.7.7 Alternative name(s): 2-oxoisovalerate oxidoreductase gamma chain 2-oxoisovalerate ferredoxin reductase subunit gamma | ||
| Gene names |
| ||
| Organism | Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133) | ||
| Taxonomic identifier | 79929 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter |
Protein attributes
| Sequence length | 24 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+). |
| Cofactor | Binds 2 4Fe-4S clusters By similarity. |
| Subunit structure | Heterotrimer of the vorA, vorB and vorC subunits. |
| Sequence similarities | Contains at least 1 4Fe-4S ferredoxin-type domain. |
| Biophysicochemical properties | pH dependence: Optimum pH is 9.7. Temperature dependence: Optimum temperature is 75 degrees Celsius. |
Ontologies
Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Domain | Repeat |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity Inferred from electronic annotation. Source: EC 4 iron, 4 sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›24 | ›24 | Ketoisovalerate oxidoreductase subunit vorC | PRO_0000099960 | |||||
Regions | |||||||||
| Domain | 4 – ›24 | ›21 | 4Fe-4S ferredoxin-type | ||||||
Sites | |||||||||
| Metal binding | 13 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 16 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 19 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
Experimental info | |||||||||
| Sequence uncertainty | 13 | 1 | |||||||
| Sequence uncertainty | 16 | 1 | |||||||
| Sequence uncertainty | 19 | 1 | |||||||
| Non-terminal residue | 24 | 1 | |||||||
Sequences
References
| [1] | "Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum." Tersteegen A., Linder D., Thauer R.K., Hedderich R. Eur. J. Biochem. 244:862-868(1997) [PubMed: 9108258] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001450. 4Fe4S_Fe_S_bd. [Graphical view] |
| PROSITE | PS00198. 4FE4S_FER_1. Partial match. PS51379. 4FE4S_FER_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | VORC_METTM | ||||||||
| Accession | Primary (citable) accession number: P80909 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


