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B2GG00 (B2GG00_KOCRD) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 22. 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
Name:aceE EMBL BAG29428.1
Ordered Locus Names:KRH_10810
OrganismKocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201) [Complete proteome] [HAMAP]
Taxonomic identifier378753 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Kocuria

Protein attributes

Sequence length912 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
B2GG00 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: D55062E42F99CD1C

FASTA912100,824
        10         20         30         40         50         60 
MSSDSNHHIL SGLTNNLQDA DAQETQEWIE SFDALIQAQG TERAQYIMRA LLQHAGTHSV 

        70         80         90        100        110        120 
GVPMVTTSDY VNTIPVDQEP EFPGNEEIER RYRAFLRWNA AVMVHRAQRP GVGVGGHISS 

       130        140        150        160        170        180 
YAGVATLYEV GLNHFFRGPE HPGGGDQVFF QGHSSPGNYA RAFLEGRLTE EQLDGFRQEK 

       190        200        210        220        230        240 
TKAPNGLPSY PHPRSLPDFW QFPTVSMGIG PMNAVYQAQY NRYLHNRGIK DTSEQHVWAF 

       250        260        270        280        290        300 
LGDGEMDEPE SRGVLQLAAN DKLDNLTFVV NCNLQRLDGP VRGNGKIIQE LEAFFRGAGW 

       310        320        330        340        350        360 
NVIKVVWGRE WDALLEADHT GELVRIMNET LDGDYQTFKA ESGGFVRDHF FARSAATKEL 

       370        380        390        400        410        420 
VADYTDEQIW NLKRGAHDYH KVYAAYKAAL EHKGQPTVIL AQGVKGYGLG PHFEARNATH 

       430        440        450        460        470        480 
QMKKLTLEDL KAFRDHLRIP ITDEQLEADL YNAPYYHPGP DSPEIKYLLE RRKELGGFLP 

       490        500        510        520        530        540 
DRPHAQPEIT LPSDRAYASG KKGSGKQMAA TTMAFVRILK DLMREKDFGH RIVPIVPDEA 

       550        560        570        580        590        600 
RTFGMDSFFP TSKIYNPNGQ NYLSVDRELM LAYKESAQGV ILHPGINEAG ATAAFTAAGT 

       610        620        630        640        650        660 
SYATHGETMI PVYIFYSMFG FQRTGDEFWA AADQMARGFI IGATAGRTTL TGEGLQHADG 

       670        680        690        700        710        720 
HSPILASTNP AVIHYDPAYG YEIAHIVKRG IEHMYGTGDE DHNVMYYLTV YNEPIHQPAE 

       730        740        750        760        770        780 
PENVDVDGIV NGIYLLKPAE TEGPRAQLLA SGVGVPWALE AQQILADEWG VSADVWSVTS 

       790        800        810        820        830        840 
WTNLRRDAMA AEQEAFMDPE AGARTPYIAQ ALAGATGPVV ATSDYASQLP DSVRQYVPND 

       850        860        870        880        890        900 
WASLGADGFG FADTRAGARR FFTIDAHSMV VRTLEMLAKR GEIDWSAPAE ALTRYQLANP 

       910 
EAGTSGNTGG DA

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References

[1]"Complete genome sequence of the soil actinomycete Kocuria rhizophila."
Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
J. Bacteriol. 190:4139-4146(2008) [PubMed: 18408034] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009152 Genomic DNA. Translation: BAG29428.1.
RefSeqYP_001854934.1. NC_010617.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2GG00.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6238333.
GenomeReviewsGene locus KRH_10810 in contig AP009152_GR.
KEGGkrh:KRH_10810.
PATRIC22182396. VBIKocRhi5258_1061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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 nameB2GG00_KOCRD
AccessionPrimary (citable) accession number: B2GG00
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: December 14, 2011
This is version 22 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