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UniProtKB/Swiss-Prot entry Q6ABX8


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

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Entry information
Entry name ODPB_LEIXX
Primary accession number Q6ABX8
Secondary accession numbers None
Integrated into Swiss-Prot on April 18, 2006
Sequence was last modified on September 13, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 25)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta
Synonym EC 1.2.4.1
Gene name
Name: pdhB
OrderedLocusNames: Lxx25060
From
Leifsonia xyli subsp. xyli [TaxID: 59736] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Micrococcineae; Microbacteriaceae; Leifsonia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CTCB07;
PubMed=15305603 [NCBI, ExPASy, EBI, Israel, Japan]
Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P., Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L., El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
"The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli subsp. xyli.";
Mol. Plant Microbe Interact. 17:827-836(2004).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
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
AE016822; AAT90114.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_063219.1; -.
3D structure databases
ModBase Q6ABX8.
Enzyme and pathway databases
BioCyc LXYL281090:LXX25060-MON; -.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
BLOCKS Q6ABX8.
Genome annotation databases
GeneID 2940400; -.
GenomeReviews AE016822_GR; Lxx25060.
KEGG lxx:Lxx25060; -.
NMPDR fig|281090.3.peg.2006; -.
Phylogenomic databases
HOGENOM Q6ABX8; -.
Genome annotation databases
CMR Q6ABX8; Lxx25060.
Other
ProtoNet Q6ABX8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   337  337     Pyruvate dehydrogenase E1 component subunit beta. PRO_0000232457
BINDING   73    73        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 337 AA [This is the length of the unprocessed precursor] Molecular weight: 36087 Da [This is the MW of the unprocessed precursor] CRC64: 2B45A895DC8D84E2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MERAPALAEP EPRVQSLPMV KALNAGLRQA LVADPKVLIL GEDVGPLGGV FRVTEGLQSE 

        70         80         90        100        110        120 
FGASRVVDTP LAEAGIVGTA IGLAMRGYRP VVEIQFNGFV FPGFDQITTQ LAKMANRHSG 

       130        140        150        160        170        180 
AVSMPVVIRI PHGGHIGAVE HHQEAPEAYF AHTAGLRIVA PSTPHDAYWM IQEAIASDDP 

       190        200        210        220        230        240 
VIFFEPMSRY WPKGEVDTLE NPLPLHASRI VRSGTDATIV AWAGMVPVAL RAAEIAAEEG 

       250        260        270        280        290        300 
RSLEVVDLRS LAPIDYAPVL RSVQKTGRLV VAQEAPGIVS VGSEVAAVVG EKAFYSLEAP 

       310        320        330 
VLRVAGFDTP FPPAKLESLY LPDADRILEV VDRSLAY 

Q6ABX8 in FASTA format

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