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B8HA79 (B8HA79_ARTCA) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. 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
Ordered Locus Names:Achl_2203
OrganismArthrobacter chlorophenolicus (strain A6 / ATCC 700700 / DSM 12829 / JCM 12360) [Complete proteome] [HAMAP]
Taxonomic identifier452863 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length913 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
B8HA79 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 0AC15CD253CA473C

FASTA913101,251
        10         20         30         40         50         60 
MAAGEDTSHI LSGLTDQLPD RDPEETAEWV ESLDALIREQ GTERAQYIMR SLLQRAGAQS 

        70         80         90        100        110        120 
VGVPMVTTTD YVNTIPVDQE APFPGNEEYE RRYRAYMRWN AAVMVHRAQR PEIGVGGHIS 

       130        140        150        160        170        180 
TYAGAATLYE VGFNHFFRGK DAPGGGDQVF FQGHASPGMY ARAFMEGRLT EEDLDGFRQE 

       190        200        210        220        230        240 
KSRAGHALSS YPHPRLMPDF WEFPTVSMGI GPMNAIYQAQ SNRYLHNRGL KDTSDQQVWA 

       250        260        270        280        290        300 
FLGDGEMDEP ESRGLLQLAA NENLDNLNFV INCNLQRLDG PVRGNGKIMQ ELEAFFRGAG 

       310        320        330        340        350        360 
WNVIKVVWGR EWDDLLTRDT NGSLVKIMNE TPDGDYQTYK AESGGFVREH FFGKDPATKD 

       370        380        390        400        410        420 
MVADLTDDQI WNLKRGGHDY RKVYAAYKAA TEFKGKPTVI LAKTVKGYGL GPHFEGRNAT 

       430        440        450        460        470        480 
HQMKKLTLDD LKKFRDHLRI PVTDEQLEQD TYRPPYYHPG TDAPEIKYMM ERRAALGGSV 

       490        500        510        520        530        540 
PERRSKHAEI VLPEAKTYEV AKRGSGKQQA ATTMAFVRLL KDLMRDKNFG KHIAPIIPDE 

       550        560        570        580        590        600 
ARTFGMDAFF PTAKIYNPKG QNYLSVDRDL VLAYKESPAG QLIHPGINEA GAVAAFTAAG 

       610        620        630        640        650        660 
TAYATHGVPL VPVYVFYSMF GFQRTGDAFW AAADQMTRGF IIGATAGRTT LTGEGLQHAD 

       670        680        690        700        710        720 
GHSPLLASTN PAVVTYDPAY GYEMGHIIRD GIERMYGPDS EDRNLMYYLT VYNEPIVQPA 

       730        740        750        760        770        780 
EPAELDVEGV IKGIYLLAPA KIDGPRTQIL ASGVSVPWAL EAQRILAEDW SVSADVWSVT 

       790        800        810        820        830        840 
SWNELRRDGL AAEEEAFLNP EQPARVPFVT QQLEGATGPV VAVSDYMKAV PDQIRQFVPN 

       850        860        870        880        890        900 
EYATLGADGF GFSDTRAAAR RYFKNDTHSI VVRALEMLAR RGEVDAGAPV KAIEKYKLLN 

       910 
VNAGTTGNTG GEA

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References

[1]"Complete sequence of chromosome of Arthrobacter chlorophenolicus A6."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A6 / ATCC 700700 / DSM 12829 / JCM 12360.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001341 Genomic DNA. Translation: ACL40171.1.
RefSeqYP_002488260.1. NC_011886.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB8HA79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7293671.
GenomeReviewsGene locus Achl_2203 in contig CP001341_GR.
KEGGach:Achl_2203.
PATRIC20991015. VBIArtChl38304_2883.

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. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB8HA79_ARTCA
AccessionPrimary (citable) accession number: B8HA79
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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