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Q59098

- ODP2_CUPNH

UniProt

Q59098 - ODP2_CUPNH

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Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Gene
pdhB, H16_A1375
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - 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

Binds 2 lipoyl cofactors covalently By similarity.

Sites

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

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: 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 complex
PRO_0000162271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-lipoyllysine By similarity
Modified residuei162 – 1621N6-lipoyllysine By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7777Lipoyl-binding 1
Add
BLAST
Domaini123 – 19573Lipoyl-binding 2
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiVKVPNIG.
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

MSQAIEIKVP DIGDYDAVPV IEVHVKPGDS INAEDALVTL ESDKATMDVP    50
SPQAGVVKDV RIKVGDNVSE GSVLVMLEAA NEPAAAPAPA AAAPAPAAAA 100
PAPAPAPAAA PAAAPAAGGG GTIEVKVPDI GDYDAVPVIE VHVKAGDTIN 150
AEDAVVTLES DKATMDVPSP QGGVVKEVKV KVGDNVAEGT LLLILEGAAA 200
SAAPAAAAAA PAPAASAPAP APAPAAAAPA PAAAPAAAPA AAGVTGKAAH 250
ASPSVRKFAR ELGVDVSRVP GTGPKGRITQ EDVQGYVKGV MSGQAAAPAQ 300
AAAAGAGGGE LGLLPWPKFD FTRFGEVESK ALSRIKKISG ANLHRNWVMI 350
PHVTNHDEAD ITELEAFRLQ LNKENEKSGI KVTMLAFMIK ATVAALKKFP 400
NFNASLDGDN LVLKKYFNIG FAADTPNGLV VPVIKDADKK GVLEISQEMS 450
ELAKLARDGK LKPDQMQGGC FSISSLGGLG GTYFTPIINA PEVAIMGVCK 500
SYQKPVWDGK QFAPRLTLPL SLSWDHRVID GAEAARFNTY FGQLLADFRR 550
ILL 553
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011S → A in AAA21599. 1 Publication
Sequence conflicti319 – 3191F → V in AAA21599. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U09865 Genomic DNA. Translation: AAA21599.1 . Frameshift.
AM260479 Genomic DNA. Translation: CAJ92511.1 .
PIRi B55514.
RefSeqi WP_011615028.1. NC_008313.1.
YP_725879.1. NC_008313.1.

3D structure databases

ProteinModelPortali Q59098.
SMRi Q59098. Positions 315-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 381666.H16_A1375.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ92511 ; CAJ92511 ; H16_A1375 .
GeneIDi 4249767.
KEGGi reh:H16_A1375.
PATRICi 35232213. VBIRalEut6770_1764.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
KOi K00627.
OMAi VKVPNIG.
OrthoDBi EOG6HQSJH.

Enzyme and pathway databases

BioCyci CNEC381666:GJUJ-1372-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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 99 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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