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A3Q1X4 (A3Q1X4_MYCSJ) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 34. 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:Mjls_3373
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length924 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
A3Q1X4 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: C852DA44C2E562F3

FASTA924103,038
        10         20         30         40         50         60 
MRQDLAQNSS TAAEHDRVRV IREGVASYLP DIDPDETSEW LESFDQLLER SGPARARYLL 

        70         80         90        100        110        120 
LRLLERSGEQ RVAIPALTST DYVNTIPTEL EPWFPGDEDV ERRYRAWIRW NAAIMVHRAQ 

       130        140        150        160        170        180 
RPGVGVGGHI STYASSAALY EVGFNHFFRG KSHSGGGDQV FIQGHASPGI YARAYLEGRL 

       190        200        210        220        230        240 
TADQLDGFRQ EHSHPGGGIP SYPHPRLMPD FWEFPTVSMG LGPMNAIYQA RFNHYLHDRG 

       250        260        270        280        290        300 
IKDTTDQHVW AFLGDGEMDE PESRGLIHVA ALEALDNLTF VVNCNLQRLD GPVRGNGKII 

       310        320        330        340        350        360 
QELESFFRGA GWNVIKVVWG REWDALLHAD RDGALVNLMN TTPDGDYQTY KANDGGYVRD 

       370        380        390        400        410        420 
HFFGRDPRTK ALVEPMTDAE IWNLKRGGHD YRKVYAAYRA AMEHKGQPTV ILAKTIKGYT 

       430        440        450        460        470        480 
LGKHFEGRNA THQMKKLALQ DLKDFRDAQR IPIGDAQLEE NPYLPPYYHP GPEAPEIRYM 

       490        500        510        520        530        540 
LDRRRALGGF VPERRTKSKA LALPSSDAYK ALKKGSGKQE VATTMATVRT FKEILRDKQI 

       550        560        570        580        590        600 
GHRIVPIIPD EARTFGMDSW FPNLKIYNRN GQLYTSVDAE LMLAYRESEV GQILHEGINE 

       610        620        630        640        650        660 
AGSVGTFIAA GTSYATHNEP MIPIYIFYSM FGFQRTGDSF WAAADQMARG FVLGATAGRT 

       670        680        690        700        710        720 
TLVGEGLQHA DGHSLLLAST NPAVVAYDPA FAYEIAYIIE SGLHRMYGEN PENVYFYLTI 

       730        740        750        760        770        780 
YNEPYVQPAE PENLDVEGLL RGIYRYRAAA EKKSNTAQIL VSGVAMPSAL KAAEMLAEEW 

       790        800        810        820        830        840 
DVAADVWSVT SWNELNRDGV QVEKDLLRHP DRPAGTPYIT TALADAAGPV VAVSDWMRAV 

       850        860        870        880        890        900 
PEQIRPWVPG TYITLGTDGF GFSDTRPAAR RFYNTDAESI TVAVLEGLAR DGNIDISVAV 

       910        920 
EAARRYEIDD VLAAPEQTSD PGVA

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000580 Genomic DNA. Translation: ABN99151.1.
RefSeqYP_001071642.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3Q1X4.
SMRA3Q1X4. Positions 80-915.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3Q1X4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000050194; EBMYCP00000048475; EBMYCG00000050189.
GeneID4879085.
GenomeReviewsGene locus Mjls_3373 in contig CP000580_GR.
KEGGmjl:Mjls_3373.
PATRIC18092932. VBIMycSp51234_3393.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
GeneTreeEBGT00050000016271.
HOGENOMHBG289271.
OMAFRQEKSH.
PhylomeDBA3Q1X4.
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 nameA3Q1X4_MYCSJ
AccessionPrimary (citable) accession number: A3Q1X4
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 34 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