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Q6A924 (Q6A924_PROAC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 46. 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:PPA0989
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP] EMBL AAT82742.1
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length917 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
Q6A924 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 5F88C41E51F3708C

FASTA917101,722
        10         20         30         40         50         60 
MIPREERGPV LNGLPTTLPD VDPEETQEWI ESLDKMVETD GPNRARIVLL KMLERARSHS 

        70         80         90        100        110        120 
RLGLSALTST DYINTIAAED EEEYPGDAEI ERNIRRLLRW NSAITVHRAQ RPGIGVGGHI 

       130        140        150        160        170        180 
STYASAVTLY EVGQNHFWRG QDAPGGGDQV FFQGHAAPGM YARAFLEGRL SEDDLDGFRQ 

       190        200        210        220        230        240 
EKSKAGHGLP SYPHPRMLPD FWQFPTVSMG LGPMNSIYQA SMNKYLTNRG VKDCADQHVW 

       250        260        270        280        290        300 
AFLGDGEMDE PESRGFLQVA ANEELDNLTF VINCNLQRLD GPVRGNGKIV QELEAVFRGA 

       310        320        330        340        350        360 
GWNVIKVIWG SGWDPLLQAD RDGALVDIMN NTRDGDYQTF KANDGAYVRE HFFGRDPRTA 

       370        380        390        400        410        420 
KMVDKWTDEQ IWALRRGGHD YRKIYNAYKA ATQFKGAPTV VLACTIKGYD LGTHFAGRNA 

       430        440        450        460        470        480 
THQMKKLALE DLKQFRDRLE IPISDKVLEA DPYRAPYFHP GADDERIQYL MERRRALGGF 

       490        500        510        520        530        540 
VPERRTRHTP LPIPAQKAFD GVKRGSGKQE VATTMAFVRL LKDLMRDKNF APHVVPIIPD 

       550        560        570        580        590        600 
EARTFGMDSF FPTIKIYNPH GQNYTPVDHE LMLSYREAKN GQIIHTGINE AGSAAAFIAA 

       610        620        630        640        650        660 
GSAYSTQGVP MVPIYLFYSM FGFQRTGDSF WAAGDQMTRG FIIGATAGRT TLTGEGTQHM 

       670        680        690        700        710        720 
DGHSPVLAAT NPAVISYDPA YSYEISHIVQ AGLEHMYGEN AEDVMYYLTV YNEPIVQPAE 

       730        740        750        760        770        780 
PEGVDAEGIV KGMYLLSKGS FEGVGEDARR VQLLASGVAV PWAIEAQQLL KGDFGVVADV 

       790        800        810        820        830        840 
WSVTSWNNLR RDAMEAEEQT FLHPEQGRRT PYITQCLADA PGPVVATTDY TCQVPDQIAQ 

       850        860        870        880        890        900 
WVPGDYASLG ADGFGFSDTR AAARRFFHID GPSMTVRALQ MLVERGEVPE DWPAKAAEKY 

       910 
DLLNVNAGAS GNAGGDA

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References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017283 Genomic DNA. Translation: AAT82742.1.
RefSeqYP_055700.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A924.
SMRQ6A924. Positions 70-905.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2931847.
GenomeReviewsGene locus PPA0989 in contig AE017283_GR.
KEGGpac:PPA0989.
NMPDRfig|267747.1.peg.977.
PATRIC23036703. VBIProAcn64440_1024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289271.
OMAFRQEKSH.
PhylomeDBQ6A924.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycPACN267747:PPA0989-MONOMER.

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 nameQ6A924_PROAC
AccessionPrimary (citable) accession number: Q6A924
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2004
Last sequence update: September 13, 2004
Last modified: December 14, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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