ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O26799

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name VORC_METTH
Primary accession number O26799
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Ketoisovalerate oxidoreductase subunit vorC
Synonyms VOR
EC 1.2.7.7
2-oxoisovalerate oxidoreductase gamma chain
2-oxoisovalerate ferredoxin reductase subunit gamma
Gene name
Name: vorC
OrderedLocusNames: MTH_703
From
Methanobacterium thermoautotrophicum [TaxID: 187420] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Delta H;
PubMed=9371463 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.";
J. Bacteriol. 179:7135-7155(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE000666; AAB85208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H69193; H69193.
RefSeq NP_275846.1; -.
3D structure databases
ModBase O26799.
Enzyme and pathway databases
BioCyc MTHE187420:MTH703-MON; -.
Ontologies
GO
GO:0043807; Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity (inferred from electronic annotation from EC).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001450; 4Fe4S_Fe_S_bd.
Graphical view of domain structure.
Pfam PF00037; Fer4; 2.
Pfam graphical view of domain structure.
PROSITE PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1470664; -.
GenomeReviews AE000666_GR; MTH_703.
KEGG mth:MTH703; -.
NMPDR fig|187420.1.peg.701; -.
Phylogenomic databases
HOGENOM O26799; -.
Genome annotation databases
CMR O26799; MTH_703.
Other
ProtoNet O26799.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Repeat; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   79  79     Ketoisovalerate oxidoreductase subunit vorC. PRO_0000099959
DOMAIN   4   33  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   40   70  31     4Fe-4S ferredoxin-type 2. 
METAL   13   13        Iron-sulfur 1 (4Fe-4S) (Potential). 
METAL   16   16        Iron-sulfur 1 (4Fe-4S) (Potential). 
METAL   19   19        Iron-sulfur 1 (4Fe-4S) (Potential). 
METAL   23   23        Iron-sulfur 2 (4Fe-4S) (Potential). 
METAL   49   49        Iron-sulfur 2 (4Fe-4S) (Potential). 
METAL   52   52        Iron-sulfur 2 (4Fe-4S) (Potential). 
METAL   55   55        Iron-sulfur 2 (4Fe-4S) (Potential). 
METAL   59   59        Iron-sulfur 1 (4Fe-4S) (Potential). 
Sequence information
Length: 79 AA [This is the length of the unprocessed precursor] Molecular weight: 8928 Da [This is the MW of the unprocessed precursor] CRC64: 9DFE9CC6A2AE943E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKAYPVINS VECKACERCI IACPRKVLQM SSKINERGYH YVEYRGEGCN GCGNCYYTCP 

        70 
EINAIEVHIE RCEDGNTDG
O26799 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!