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B0UGS0 (B0UGS0_METS4) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 26. 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:M446_1239
OrganismMethylobacterium sp. (strain 4-46) [Complete proteome] [HAMAP]
Taxonomic identifier426117 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length884 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
B0UGS0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 002A3706743F9BC0

FASTA88499,096
        10         20         30         40         50         60 
MDSTRDPDPI ETREWLDSLD GVLEVEGPDR AHFLIEQVIE EARKKGAPVP YSANTAYLNT 

        70         80         90        100        110        120 
IPLEAQAKHP GDRAIEHRIR SAIRWNAIAI ILRNNKDSSE LGGHIASFQS AATLYDTGFM 

       130        140        150        160        170        180 
HFWRGASDGH GGDLIYVQGH CSPGIYARAF LEGRITEEQL LSFRQEVSGK GLSSYPHPWL 

       190        200        210        220        230        240 
MPDFWQFPTV SMGLGPLMAI YQARYLRYLH HRGLADTDRR KVWAFMGDGE MDEPESLGAI 

       250        260        270        280        290        300 
SLAAREKLDN LVFVINCNLQ RLDGPVRGNG KIVQELEANF RGAGWNVIKV LWGSGWDALL 

       310        320        330        340        350        360 
ARDTSGMLAR LMTECVDGEY QDFKSKNGAY IREHFFGRYP ETKALVADWS DDDIWRLTRG 

       370        380        390        400        410        420 
GHDPSKVYAA YHAAVNHKGQ PTVILAKTVK GYGMGEAGEA QNITHQQKKM GEAVLRQFRD 

       430        440        450        460        470        480 
RFQIDLTDDK LTEIPFIRFP DGSPEHRYLM ARRQALGGPL PARRQKSQSL EVPPLSAFSA 

       490        500        510        520        530        540 
QLKETAGREI STTMAFVRVL NTLLRDKEIG KRIVPIVPDE SRTFGMEGMF RQFGIFSQVG 

       550        560        570        580        590        600 
QLYRPEDANQ LMYYKEDKNG QMLQEGINEA GAMSSWIAAA TSYSHSNAPT IPFYIYYSMF 

       610        620        630        640        650        660 
GFQRVGDLAW AAGDLRARGF LIGGTAGRTT LNGEGLQHED GHSHLFSATI PNCVSYDPTF 

       670        680        690        700        710        720 
SYEVAVIVQD GLRRMYGEQE DVFYYITVMN ENYEHPGMPD GAQEGIIKGM YLFREGKGKG 

       730        740        750        760        770        780 
PRVQLLGSGT ILREVIAGAE LLEKDFGIVA DIWSCPSFTE LARDAMAVER WNMLHPTETP 

       790        800        810        820        830        840 
RKSYVETCLS GRSGPVIAAS DYMRLFADQI RPFVPARYKV LGTDGFGRSD YRVRLRDFFE 

       850        860        870        880 
VDRRWVAVAA LKSLAEDKRV PTAKVVEAIA KYGIDPGKPA PWTV 

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References

[1]"Complete sequence of chromosome of Methylobacterium sp. 4-46."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000943 Genomic DNA. Translation: ACA15763.1.
RefSeqYP_001768197.1. NC_010511.1.

3D structure databases

ProteinModelPortalB0UGS0.
SMRB0UGS0. Positions 57-881.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0UGS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6134155.
GenomeReviewsGene locus M446_1239 in contig CP000943_GR.
KEGGmet:M446_1239.
PATRIC22583777. VBIMetSp32184_1254.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289271.
OMADRHFVVL.
ProtClustDBPRK09405.

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. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB0UGS0_METS4
AccessionPrimary (citable) accession number: B0UGS0
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)