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C4K7S2 (C4K7S2_HAMD5) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length531 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 By similarity. RuleBase RU361137

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. RuleBase RU361137

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. RuleBase RU361137

Binds 2 lipoyl cofactors covalently By similarity. RuleBase RU361137

Binds 3 lipoyl cofactors covalently By similarity. RuleBase RU361137

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. RuleBase RU361137

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family. RuleBase RU361137

Contains 2 lipoyl-binding domains. RuleBase RU361137

Ontologies

Sequences

Sequence LengthMass (Da)Tools
C4K7S2 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 1094740AB48E9E03

FASTA53157,709
        10         20         30         40         50         60 
MVIEIKMPDI GTDTPEVIEI MVKVGDVVVP EQTLLCVEGD KASMDIPSPQ EGTIKEIKVS 

        70         80         90        100        110        120 
VGDKVETGKL IMLFESSTEA VPEKKGKTQV PAPAIPAQEN TKTVSLPDVG SDELEVTEIL 

       130        140        150        160        170        180 
VKVGDSVTEE QSLITVEGDK ASMEVPAPFS GTVKEIQIKT GDKVKTGSMI MIMNTIEKIT 

       190        200        210        220        230        240 
PAPDQKIQKT ADALPEQKPE IPPSKPSAPS NTTTSIEKTT PSFTEEAYTH ATPVIRRLAR 

       250        260        270        280        290        300 
ELGVNLEKVA GTGRKGRILK EDVQSYVKNA VQTAESASSG QGNLTPLLPW PKIDFNQFGE 

       310        320        330        340        350        360 
TEEIALTRIQ KMSGDNLSRN WVMIPHVTQF DETDITDLED FRKKQNIEAE KRKLDVKITP 

       370        380        390        400        410        420 
VVFMMKAVAQ ALKTFPRFNS SLSLDGKKLI LKKYINIGVA VDTPNGLVVP VFRDVNKKGV 

       430        440        450        460        470        480 
IELSKELMLI SQKARSGKLT ASDMQGGCFT ISSLGGIGGT AFTPIVNAPE VAILGVSKSA 

       490        500        510        520        530 
IKPIWNGKEF LPRLMLPLSL SFDHRVIDGA AGARFVSHIS VIMADIRRLI M 

« Hide

References

[1]"Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5AT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001277 Genomic DNA. Translation: ACQ68615.1.
RefSeqYP_002924763.1. NC_012751.1.

3D structure databases

ProteinModelPortalC4K7S2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING572265.HDEF_2043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ68615; ACQ68615; HDEF_2043.
GeneID7951639.
KEGGhde:HDEF_2043.
PATRIC31975547. VBICanHam112931_2023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
KOK00627.
OMATEIMVAV.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycHDEF572265:GJAB-2066-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC4K7S2_HAMD5
AccessionPrimary (citable) accession number: C4K7S2
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)