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Q8K9T8

- ODP2_BUCAP

UniProt

Q8K9T8 - ODP2_BUCAP

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei375 – 3751Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-210-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
Gene namesi
Name:aceF
Ordered Locus Names:BUsg_200
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N6-lipoyllysineBy similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi198804.BUsg200.

Structurei

3D structure databases

ProteinModelPortaliQ8K9T8.
SMRiQ8K9T8. Positions 1-70, 171-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6868Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
KOiK00627.
OMAiCIINRIG.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K9T8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPDIGLEEVE VTEILVKIGE EIKLDQGLIT VEGDKASMEI PSPISGIVKD
60 70 80 90 100
ITIKIGEKVK TSSIIMIFKV NNLNSIKNEK DLNYIKTEKK LNENFLEEKK
110 120 130 140 150
DIKKIVLVHA TPVVRRLARH LNVDLKNITP SGPKNRILKE DIELYIRNNT
160 170 180 190 200
SNKSSFNIEK NNTTNFHKDL FNEIPITNIQ QIIGKNLHQN WVNIPHVTQF
210 220 230 240 250
DEVNITLLEE FRHKYNTEKK QKNNMCSKIT ILPFIIKSVA YGLLEFPIFN
260 270 280 290 300
SSLSVNKKTI FLKKYVNVGI AVDVQNALFV PVLKNVDKKN IANLSSELIF
310 320 330 340 350
LSKKAHENKL DASDMKDGCF TISNLGGIGG SWFSPIINSP EVAILGVSKA
360 370 380 390 400
LIKPLWNGKE FIPSLMLPLS LSYDHRVING ADAARFLTFI GKMLSDIRFL

IM
Length:402
Mass (Da):45,421
Last modified:November 8, 2002 - v2
Checksum:i1F784349E26E5643
GO

Sequence cautioni

The sequence AAM67764.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67764.1. Different initiation.
RefSeqiNP_660553.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67764; AAM67764; BUsg_200.
GeneIDi1005397.
KEGGibas:BUsg200.
PATRICi21247187. VBIBucAph100086_0207.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67764.1 . Different initiation.
RefSeqi NP_660553.1. NC_004061.1.

3D structure databases

ProteinModelPortali Q8K9T8.
SMRi Q8K9T8. Positions 1-70, 171-402.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198804.BUsg200.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM67764 ; AAM67764 ; BUsg_200 .
GeneIDi 1005397.
KEGGi bas:BUsg200.
PATRICi 21247187. VBIBucAph100086_0207.

Phylogenomic databases

eggNOGi COG0508.
KOi K00627.
OMAi CIINRIG.
OrthoDBi EOG610413.

Enzyme and pathway databases

BioCyci BAPH198804:GHMG-210-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiODP2_BUCAP
AccessioniPrimary (citable) accession number: Q8K9T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: October 1, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3