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A1UIG0 (A1UIG0_MYCSK) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 35. 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:Mkms_3424
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length929 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
A1UIG0 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 2F56B1BF16B4A372

FASTA929103,615
        10         20         30         40         50         60 
MTTEFVRQDL AQNSSTAAEH DRVRVIREGV ASYLPDIDPD ETSEWLESFD QLLERSGPAR 

        70         80         90        100        110        120 
ARYLLLRLLE RSGEQRVAIP ALTSTDYVNT IPTELEPWFP GDEDVERRYR AWIRWNAAIM 

       130        140        150        160        170        180 
VHRAQRPGVG VGGHISTYAS SAALYEVGFN HFFRGKSHSG GGDQVFIQGH ASPGIYARAY 

       190        200        210        220        230        240 
LEGRLTADQL DGFRQEHSHP GGGIPSYPHP RLMPDFWEFP TVSMGLGPMN AIYQARFNHY 

       250        260        270        280        290        300 
LHDRGIKDTT DQHVWAFLGD GEMDEPESRG LIHVAALEAL DNLTFVVNCN LQRLDGPVRG 

       310        320        330        340        350        360 
NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADRDGAL VNLMNTTPDG DYQTYKANDG 

       370        380        390        400        410        420 
GYVRDHFFGR DPRTKALVEP MTDAEIWNLK RGGHDYRKVY AAYRAAMEHK GQPTVILAKT 

       430        440        450        460        470        480 
IKGYTLGKHF EGRNATHQMK KLALQDLKDF RDAQRIPIGD AQLEENPYLP PYYHPGPEAP 

       490        500        510        520        530        540 
EIRYMLDRRR ALGGFVPERR TKSKALALPS SDAYKALKKG SGKQEVATTM ATVRTFKEIL 

       550        560        570        580        590        600 
RDKQIGHRIV PIIPDEARTF GMDSWFPNLK IYNRNGQLYT SVDAELMLAY RESEVGQILH 

       610        620        630        640        650        660 
EGINEAGSVG TFIAAGTSYA THNEPMIPIY IFYSMFGFQR TGDSFWAAAD QMARGFVLGA 

       670        680        690        700        710        720 
TAGRTTLVGE GLQHADGHSL LLASTNPAVV AYDPAFAYEI AYIIESGLHR MYGENPENVY 

       730        740        750        760        770        780 
FYLTIYNEPY VQPAEPENLD VEGLLRGIYR YRAAAEKKSN TAQILVSGVA MPSALKAAEM 

       790        800        810        820        830        840 
LAEEWDVAAD VWSVTSWNEL NRDGVQVEKD LLRHPDRPAG TPYITTALAD AAGPVVAVSD 

       850        860        870        880        890        900 
WMRAVPEQIR PWVPGTYITL GTDGFGFSDT RPAARRFYNT DAESITVAVL EGLARDGNID 

       910        920 
ISVAVEAARR YEIDDVLAAP EQTSDPGVA 

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References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL92618.1.
RefSeqYP_939408.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UIG0.
SMRA1UIG0. Positions 85-920.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1UIG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000057620; EBMYCP00000055844; EBMYCG00000057615.
GeneID4611352.
GenomeReviewsGene locus Mkms_3424 in contig CP000518_GR.
KEGGmkm:Mkms_3424.
PATRIC18105828. VBIMycSp70743_3943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
GeneTreeEBGT00050000016271.
HOGENOMHBG289271.
OMAFRQEKSH.
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. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA1UIG0_MYCSK
AccessionPrimary (citable) accession number: A1UIG0
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)