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A9WP69 (A9WP69_RENSM) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component PIRNR PIRNR000156
EC=1.2.4.1 PIRNR PIRNR000156
Gene names
Ordered Locus Names:RSal33209_1106
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP] EMBL ABY22844.1
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Renibacterium

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. PIRNR PIRNR000156

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. PIRNR PIRNR000156

Cofactor

Thiamine pyrophosphate By similarity. PIRNR PIRNR000156

Sequences

Sequence LengthMass (Da)Tools
A9WP69 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: E3465A5E052B7E46

FASTA919101,954
        10         20         30         40         50         60 
MDVAAGEENS QILSVLTNQL PDRDPDETAE WIESLDSLIK EQGTERAQFI MRSLLQRAGA 

        70         80         90        100        110        120 
QSVGVPMVTT TDYVNTIPVD QEPEFPGDEE IERKYRAWLR WNAAIMVHRA QRPDIGVGGH 

       130        140        150        160        170        180 
ISTYAGAATL YEVGFNHFFR GKDHPGGGDQ IYFQGHASPG MYARAFMEGR LSEEDLDGFR 

       190        200        210        220        230        240 
QEKSKEGHGL SSYPHPRLMP DFWEFPTVSM GIGPMNAIYQ AQSNRYLENR GIKDTSESQV 

       250        260        270        280        290        300 
WAFLGDGEMD EPESRGLLQL AANDKLDNLN FVINCNLQRL DGPVRGNGKI MQELEAFFRG 

       310        320        330        340        350        360 
AGWNVIKVVW GREWDSLLEK DNDGALVDIM NTTVDGDYQT YKAESGGFVR EHFFGQSPQT 

       370        380        390        400        410        420 
KEMVADMTDE DIWNLKRGGH DYRKVYAAYK AAVEFKGKPT VILAHTVKGY GLGTHFEGRN 

       430        440        450        460        470        480 
ATHQMKKLTL QDLKDFRDHL RIPITDEQLE ANPYHPPYYH PGMDTPEIKY LMERRLALGG 

       490        500        510        520        530        540 
FVPERRHKHT ELTLPGDKAY EVANRGSGKQ MAATTMAFVR LLKDLMRDKE FGKRVVPIIP 

       550        560        570        580        590        600 
DEARTFGMDS FFPTAKIYNP KGQNYLSVDR DLVLAYKESP SGQIVHAGIN EAGSVAAFTA 

       610        620        630        640        650        660 
AGTAYATHGE PLIPIYVFYS MFGFQRTGDG LWAAADQMSR GFVVGATAGR TTLTGEGLQH 

       670        680        690        700        710        720 
ADGHSLILAS TNPAVISYDP AYGYEIGHIV RSGLERMYGT NSSFTEEERN VMYYLLVYNE 

       730        740        750        760        770        780 
PLLQPAAPEE LDVEGIVKGI YLLAPAKVDG PRTQLLASGV AVPWALEAQK ILADEWGVSA 

       790        800        810        820        830        840 
DVWSVTSWTE LRRDGLAAEE EQFLNPAAPV RTPFVTEQLA GATGPIVAVT DHMKAVPDQI 

       850        860        870        880        890        900 
RQFVPNEFAT LGADGFGFSD TRAAARRFFK IDSHSVVVRA LEMLARRGEV DAQAPIQAIE 

       910 
KYRLLDVNAG TTGNAGGDS

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References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed: 18723615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000910 Genomic DNA. Translation: ABY22844.1.
RefSeqYP_001624258.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WP69.
SMRA9WP69. Positions 71-907.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9WP69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5822194.
GenomeReviewsGene locus RSal33209_1106 in contig CP000910_GR.
KEGGrsa:RSal33209_1106.
PATRIC23075435. VBIRenSal21953_1138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289271.
OMAFRQEKSH.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycRSAL288705:RSAL33209_1106-MONOMER.

Family and domain databases

InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK00163.
PANTHERPTHR11624:SF37. PTHR11624:SF37. 1 hit.
PfamPF00456. Transketolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA9WP69_RENSM
AccessionPrimary (citable) accession number: A9WP69
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info