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Q8FNK1 (Q8FNK1_COREF) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 55. 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:CE2143
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length933 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
Q8FNK1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B960C8852D3A3A60

FASTA933104,352
        10         20         30         40         50         60 
MKNIPTGGVE MADQAKLGGK PTDDTNFAMI RDGVASYLND SDPEETKEWM DSLDGLLQDS 

        70         80         90        100        110        120 
SPERARYLML RLLERASAKR VPLPPMTSTD YVNTIPTSME PDFPGDEEME KRYRRWMRWN 

       130        140        150        160        170        180 
AAIMVHRAQR PGIGVGGHIS TYAGAAPLYE VGFNHFFRGK DHPGGGDQVF FQGHASPGMY 

       190        200        210        220        230        240 
ARAFLEGRLT ESDLDSFRQE VSYEGGGIPS YPHPHGMPDF WEFPTVSMGL GPMDAIYQAR 

       250        260        270        280        290        300 
FNRYLHNRGI KDTSEQHVWA FLGDGEMDEP ESRGLIHQAA LNNLDNLTFV INCNLQRLDG 

       310        320        330        340        350        360 
PVRGNTKIIQ ELESFFRGAG WSVIKVIWGR EWDELLEKDQ DGALVEVMNN TSDGDYQTFK 

       370        380        390        400        410        420 
ANDGAYVREH FFGRDPRTLK LVEDMTDEEI WKLPRGGHDY RKVYAAYKRA LETKDRPTVI 

       430        440        450        460        470        480 
LAHTIKGYGL GHNFEGRNAT HQMKKLTLDD LKLFRDKQGL PITDEELEKD PYLPPYYHPG 

       490        500        510        520        530        540 
EDAPEIKYMK ERRQALGGFL PERREKYEPL QVPPLDKLRS VRKGSGKQQV ATTMATVRTF 

       550        560        570        580        590        600 
KELMRDKNLA DRLVPIIPDE ARTFGLDSWF PTLKIYNPHG QNYVPVDHDL MLSYREAKDG 

       610        620        630        640        650        660 
QILHEGINEA GSVASFIAAG TSYATHGEAM IPLYIFYSMF GFQRTGDGIW AAADQMTRGF 

       670        680        690        700        710        720 
LLGATAGRTT LTGEGLQHMD GHSPILASTN PGVETYDPAF SYEIAHLVHR GIDRMYGPGK 

       730        740        750        760        770        780 
GENVIYYLTI YNEPTPQPAE PEDLDVEGLH KGIYLYDKAA EGEGHEASIL ASGIGMQWAL 

       790        800        810        820        830        840 
RARDILAEDY GIRANIFSAT SWVELARDGA RRNLEALRNP GADVGEAFVT TQLKKGSGPY 

       850        860        870        880        890        900 
VAVSDFATDL PNQIREWVPG DYIVLGADGF GFSDTRPAAR RYFNIDAESI VVAVLRGLVR 

       910        920        930 
EGVIDASVAA HAAEKYKLSD PTAPQVDPDA PIE

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References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000035 Genomic DNA. Translation: BAC18953.1.
RefSeqNP_738753.1. NC_004369.1.

3D structure databases

HSSPHSSP built from PDB template 1L8A based on UniProtKB P06958.
ProteinModelPortalQ8FNK1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1033059.
GenomeReviewsGene locus CE2143 in contig BA000035_GR.
KEGGcef:CE2143.
PATRIC21490419. VBICorEff9312_2123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289271.
OMAFRQEKSH.
PhylomeDBQ8FNK1.
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 nameQ8FNK1_COREF
AccessionPrimary (citable) accession number: Q8FNK1
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 55 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