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UniProtKB/Swiss-Prot entry P35489

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

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Entry information
Entry name ODP2_ACHLA
Primary accession number P35489
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Synonyms EC 2.3.1.12
E2
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Gene name
Name: pdhC
From
Acholeplasma laidlawii [TaxID: 2148] 
Taxonomy Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae; Acholeplasma.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1735725 [NCBI, ExPASy, EBI, Israel, Japan]
Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii.";
J. Bacteriol. 174:1388-1396(1992).
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
M81753; AAA21909.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C42653; C42653.
3D structure databases
HSSP P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P35489.
Ontologies
GO
GO:0004742; Molecular function: dihydrolipoyllysine-residue acetyltransferase activity (inferred from electronic annotation from EC).
GO:0031405; Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (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.
IPR004167; E3_bd.
Graphical view of domain structure.
Gene3D G3DSA:4.10.320.10; E3_bd; 1.
Pfam PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 2.
PF02817; E3_binding; 1.
Pfam graphical view of domain structure.
ProDom PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS50968; BIOTINYL_LIPOYL; 2.
PS00189; LIPOYL; 2.
PROSITE graphical view of domain structure (profiles).
ProtoNet P35489.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Direct protein sequencing; Glycolysis; Lipoyl; Repeat; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   544  544     Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex. PRO_0000162270
DOMAIN   1    75  75     Lipoyl-binding 1. 
DOMAIN   114   187  74     Lipoyl-binding 2. 
ACT_SITE   516   516        Potential. 
BINDING   42    42        Lipoyl (covalent) (By similarity). 
BINDING   154   154        Lipoyl (covalent) (By similarity). 
Sequence information
Length: 544 AA [This is the length of the unprocessed precursor] Molecular weight: 57261 Da [This is the MW of the unprocessed precursor] CRC64: 81E92D869CFD5424 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP VDGTIVSLGA 

        70         80         90        100        110        120 
KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA APQVAAPAAS GDIYDFKFAD 

       130        140        150        160        170        180 
IGEGIHEGTI LQWNFKVGDK VKEGETLVVV ETDKVNAELP SPVDGTILKL GKAEGEVIHV 

       190        200        210        220        230        240 
GETVVLIGQN GATLEQAQAP KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK 

       250        260        270        280        290        300 
VLASPVARKL ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS 

       310        320        330        340        350        360 
VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD ALVNFRNEAK 

       370        380        390        400        410        420 
GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE VYIKKFINLG MAVDTPDGLI 

       430        440        450        460        470        480 
VPNIKNADRL SVFELASQVR SLADDTIARK ISMDQQTGGT FTITNFGSAG IAFGTPVINY 

       490        500        510        520        530        540 
PELAILGIGK IDRKPWVVGN EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL 


LLLS
P35489 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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