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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhB

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 4 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).

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 2 lipoyl cofactors covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei526 – 5261Sequence 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

BioCyciCNEC381666:GJUJ-1372-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:pdhB
Ordered Locus Names:H16_A1375
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-lipoyllysinePROSITE-ProRule annotationBy similarity
Modified residuei162 – 1621N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi381666.H16_A1375.

Structurei

3D structure databases

ProteinModelPortaliQ59098.
SMRiQ59098. Positions 315-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 7875Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini122 – 19675Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.
OrthoDBiEOG6HQSJH.

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAIEIKVP DIGDYDAVPV IEVHVKPGDS INAEDALVTL ESDKATMDVP
60 70 80 90 100
SPQAGVVKDV RIKVGDNVSE GSVLVMLEAA NEPAAAPAPA AAAPAPAAAA
110 120 130 140 150
PAPAPAPAAA PAAAPAAGGG GTIEVKVPDI GDYDAVPVIE VHVKAGDTIN
160 170 180 190 200
AEDAVVTLES DKATMDVPSP QGGVVKEVKV KVGDNVAEGT LLLILEGAAA
210 220 230 240 250
SAAPAAAAAA PAPAASAPAP APAPAAAAPA PAAAPAAAPA AAGVTGKAAH
260 270 280 290 300
ASPSVRKFAR ELGVDVSRVP GTGPKGRITQ EDVQGYVKGV MSGQAAAPAQ
310 320 330 340 350
AAAAGAGGGE LGLLPWPKFD FTRFGEVESK ALSRIKKISG ANLHRNWVMI
360 370 380 390 400
PHVTNHDEAD ITELEAFRLQ LNKENEKSGI KVTMLAFMIK ATVAALKKFP
410 420 430 440 450
NFNASLDGDN LVLKKYFNIG FAADTPNGLV VPVIKDADKK GVLEISQEMS
460 470 480 490 500
ELAKLARDGK LKPDQMQGGC FSISSLGGLG GTYFTPIINA PEVAIMGVCK
510 520 530 540 550
SYQKPVWDGK QFAPRLTLPL SLSWDHRVID GAEAARFNTY FGQLLADFRR

ILL
Length:553
Mass (Da):56,582
Last modified:January 23, 2007 - v2
Checksum:i280424CA0475D9E3
GO

Sequence cautioni

The sequence AAA21599.1 differs from that shown. Reason: Frameshift at positions 229 and 273. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011S → A in AAA21599 (PubMed:8021225).Curated
Sequence conflicti319 – 3191F → V in AAA21599 (PubMed:8021225).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09865 Genomic DNA. Translation: AAA21599.1. Frameshift.
AM260479 Genomic DNA. Translation: CAJ92511.1.
PIRiB55514.
RefSeqiWP_011615028.1. NC_008313.1.
YP_725879.1. NC_008313.1.

Genome annotation databases

EnsemblBacteriaiCAJ92511; CAJ92511; H16_A1375.
GeneIDi4249767.
KEGGireh:H16_A1375.
PATRICi35232213. VBIRalEut6770_1764.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09865 Genomic DNA. Translation: AAA21599.1. Frameshift.
AM260479 Genomic DNA. Translation: CAJ92511.1.
PIRiB55514.
RefSeqiWP_011615028.1. NC_008313.1.
YP_725879.1. NC_008313.1.

3D structure databases

ProteinModelPortaliQ59098.
SMRiQ59098. Positions 315-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.H16_A1375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ92511; CAJ92511; H16_A1375.
GeneIDi4249767.
KEGGireh:H16_A1375.
PATRICi35232213. VBIRalEut6770_1764.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.
OrthoDBiEOG6HQSJH.

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-1372-MONOMER.

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase."
    Hein S., Steinbuechel A.
    J. Bacteriol. 176:4394-4408(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Entry informationi

Entry nameiODP2_CUPNH
AccessioniPrimary (citable) accession number: Q59098
Secondary accession number(s): Q0KBW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 106 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.