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 Q9R9N5


[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 ODPA_RHIME
Primary accession number Q9R9N5
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 51)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha
Synonym EC 1.2.4.1
Gene name
Name: pdhA
Synonyms: pdhAalpha
OrderedLocusNames: R01445
ORFNames: SMc01030
From
Rhizobium meliloti (Sinorhizobium meliloti) [TaxID: 382] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=RCR2011 / SU47;
PubMed=10796014 [NCBI, ExPASy, EBI, Israel, Japan]
Cabanes D., Boistard P., Batut J.;
"Symbiotic induction of pyruvate dehydrogenase genes from Sinorhizobium meliloti.";
Mol. Plant Microbe Interact. 13:483-493(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294398; PubMed=11481430 [NCBI, ExPASy, EBI, Israel, Japan]
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021.";
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
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.
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
AF190792; AAF04587.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591688; CAC46024.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_385551.1; -.
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
ModBase Q9R9N5.
Enzyme and pathway databases
BioCyc SMEL266834:SMC01030-MON; -.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS Q9R9N5.
Genome annotation databases
GeneID 1233098; -.
GenomeReviews AL591688_GR; R01445.
KEGG sme:SMc01030; -.
NMPDR fig|266834.1.peg.2739; -.
Phylogenomic databases
HOGENOM Q9R9N5; -.
Genome annotation databases
CMR Q9R9N5; R01445.
Other
ProtoNet Q9R9N5.
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   348  348     Pyruvate dehydrogenase E1 component subunit alpha. PRO_0000162202
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 38113 Da [This is the MW of the unprocessed precursor] CRC64: 671DBC015C03CC78 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPRKSASVS SRKTAAKPAK KDFAGGTIAE FSKEDDLKAY REMLLIRRFE EKAGQLYGMG 

        70         80         90        100        110        120 
FIGGFCHLYI GQEAVVVGMQ LALKEGDQVI TGYRDHGHML ACGMSARGVM AELTGRRGGL 

       130        140        150        160        170        180 
SKGKGGSMHM FSKEKHFYGG HGIVGAQVSL GTGLAFANRY RGNDNVSLAY FGDGAANQGQ 

       190        200        210        220        230        240 
VYESFNMAAL WKLPVIYIVE NNRYAMGTSV SRASAQTDFS QRGASFGIPG YQVDGMDVRA 

       250        260        270        280        290        300 
VKAAADEAVE HCRSGKGPII LEMLTYRYRG HSMSDPAKYR SKDEVQKMRS EHDPIEQVKA 

       310        320        330        340 
RLTDKGWATE DELKQIDKEV RDIVADSADF AQSDPEPDVS ELYTDILL 

Q9R9N5 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!