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UniProtKB/Swiss-Prot entry Q9N0F1

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

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Entry information
Entry name ODO2_PIG
Primary accession number Q9N0F1
Secondary accession numbers None
Integrated into Swiss-Prot on September 26, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 53)
Name and origin of the protein
Protein name Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial [Precursor]
Synonyms EC 2.3.1.61
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2
E2K
E2o
PE2o
Gene name
Name: DLST
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS.
TISSUE=Brain cortex, and Heart;
PubMed=10806400 [NCBI, ExPASy, EBI, Israel, Japan]
Koike K., Suematsu T., Ehara M.;
"Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex.";
Eur. J. Biochem. 267:3005-3016(2000).
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
AB035206; BAA95700.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_999562.1; -.
UniGene Ssc.2730
3D structure databases
HSSP P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q9N0F1.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0031405; Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR000089; Biotin_lipoyl.
IPR006255; SucB.
Graphical view of domain structure.
Pfam PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
Pfam graphical view of domain structure.
ProDom PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01347; sucB; 1.
PROSITE PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9N0F1.
ProtoNet Q9N0F1.
Genome annotation databases
GeneID 397690; -.
KEGG ssc:397690; -.
Phylogenomic databases
HOVERGEN Q9N0F1; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Direct protein sequencing; Lipoyl; Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    68  68     Mitochondrion. 
CHAIN   69   455  387     Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial. PRO_0000020474
DOMAIN   72   144  73     Lipoyl-binding. 
REGION   221   453  233     Catalytic. 
COMPBIAS   151   215  65     Pro-rich. 
ACT_SITE   426   426        Potential. 
ACT_SITE   430   430        Potential. 
BINDING   111   111        Lipoyl (covalent) (Potential). 
MUTAGEN   374   374        S->A: Loss of activity. 
MUTAGEN   426   426        H->C: 16% of activity. 
MUTAGEN   430   430        D->A,E,N: Loss of activity. 
MUTAGEN   451   453        LLL->AAA,DDD: Loss of activity. 
Sequence information
Length: 455 AA [This is the length of the unprocessed precursor] Molecular weight: 48977 Da [This is the MW of the unprocessed precursor] CRC64: 563B5E7455C842FA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI SNSSVLNVRF 

        70         80         90        100        110        120 
FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE DEVVCEIETD KTSVQVPSPA 

       130        140        150        160        170        180 
NGVIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA 

       190        200        210        220        230        240 
SIPTQMPPVP SPPQPLTSKP VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL 

       250        260        270        280        290        300 
KEAQNTCAML TTFNEIDMSN IQDMRARHKE AFLKKHNLKL GFMSAFVKAS AFALQEQPVV 

       310        320        330        340        350        360 
NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS ELGEKARKNE 

       370        380        390        400        410        420 
LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA IVDRPVAVGG KVEIRPMMYV 

       430        440        450 
ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL
Q9N0F1 in FASTA format

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