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Q2L1F5 (Q2L1F5_BORA1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 41. 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 CAJ49271.1
Ordered Locus Names:BAV1663
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length901 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
Q2L1F5 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: D628110F14DDB1A4

FASTA901100,708
        10         20         30         40         50         60 
MSSPAQAGGL LAVNDEDTQE TQEWLEALAA VLDREGPQRA HYLLERLIDE ARRSGAHIPF 

        70         80         90        100        110        120 
SPNTAYVNTI PPGLEPTHPG NLELEARIRS YVRWNAMAMV VKANKHNPPD GGDLGGHIAS 

       130        140        150        160        170        180 
FASLATMIGC GQNHFWHAES EDHGGDLVYF QGHTSPGMYG RAYLEGRLTE DQLNHFRQEV 

       190        200        210        220        230        240 
DGKGLSSYPH PKLMPDFWQF PTVSMGLGPL MAIYQARFLK YLHARGIADT SKRKVWVFCG 

       250        260        270        280        290        300 
DGEMDEPESL GAIALAAREK LDNLVFVINC NLQRLDGPVR GNGKIIQELE GDFRGSGWNV 

       310        320        330        340        350        360 
IKLIWGGYWD PLLAHDKEGI LRKIMEETVD GEYQAYKAND GKFVREHFFG KHPKLLEAVA 

       370        380        390        400        410        420 
RMSDEDIWRL NRGGHDPHKV YAAFDAANKH KGQPTVILAK TIKGYGMGQV GQAKNPTHQQ 

       430        440        450        460        470        480 
KKLELESIRE FRDRFGIPIA DDQLEKLPYF KPAEDSPEMK YLHERRKALG GYLPKRRQKA 

       490        500        510        520        530        540 
DEVLKVPALD AFKAVLEPTA EGREISTTQA FVRVLNQVLR DKQIGPRVVP ILADESRTFG 

       550        560        570        580        590        600 
MEGLFRQIGI YAPEGQKYTP VDKDQVMYYR EASDGQLLQE GINEAGAMSS WIAAATSYST 

       610        620        630        640        650        660 
NNRIMVPFYI YYSMFGFQRV GDLAWAAGDM QARGFLLGGT AGRTTLNGEG LQHEDGHSHL 

       670        680        690        700        710        720 
LASTIPNCVS YDPTFAHELA VIIQHGMKRM VEDQENVYYY LTVMNENYPQ PGLKAGDEEG 

       730        740        750        760        770        780 
IIKGMYKLQS KGKGKARVQL MGSGTILREV MAAQDLLEAD WGVASDVWSV TSFTELRRNG 

       790        800        810        820        830        840 
LDVERFNLLN PEQPAQVAYV TEQLSSTDGP IIASTDYMKL FADQIRPFVP KGREYKVLGT 

       850        860        870        880        890        900 
DGFGRSDFRS KLREHFEVDR HFVVLAALKA LADEGKVPVT KVAEAIKKYG INPNKANPQY 


A

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References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM167904 Genomic DNA. Translation: CAJ49271.1.
RefSeqYP_786181.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L1F5.
SMRQ2L1F5. Positions 66-901.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2L1F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6265553.
GenomeReviewsGene locus BAV1663 in contig AM167904_GR.
KEGGbav:BAV1663.
NMPDRfig|521.1.peg.1752.
PATRIC21129508. VBIBorAvi43433_1675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289271.
OMADRHFVVL.
ProtClustDBPRK09405.

Family and domain databases

InterProIPR004660. 2-oxoA_DH_E1.
IPR001849. Pleckstrin_homology.
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.
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ2L1F5_BORA1
AccessionPrimary (citable) accession number: Q2L1F5
Entry history
Integrated into UniProtKB/TrEMBL: March 7, 2006
Last sequence update: March 7, 2006
Last modified: December 14, 2011
This is version 41 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