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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: -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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei526Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

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
Proteomesi
  • UP000008210 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622711 – 553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44N6-lipoyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei162N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

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
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 78Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST75
Domaini122 – 196Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST75
Domaini250 – 287Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiENOG4107QSN Bacteria
COG0508 LUCA
HOGENOMiHOG000281562
KOiK00627
OMAiTMEFESF

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR006256 AcTrfase_Pyrv_DH_cplx
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PANTHERiPTHR43178:SF2 PTHR43178:SF2, 3 hits
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 2 hits
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 2 hits
TIGRFAMsiTIGR01348 PDHac_trf_long, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit

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 differs from that shown. Reason: Frameshift at positions 229 and 273.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201S → A in AAA21599 (PubMed:8021225).Curated1
Sequence conflicti319F → V in AAA21599 (PubMed:8021225).Curated1

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

Genome annotation databases

EnsemblBacteriaiCAJ92511; CAJ92511; H16_A1375
KEGGireh:H16_A1375
PATRICifig|381666.6.peg.1764

Similar proteinsi

Entry informationi

Entry nameiODP2_CUPNH
AccessioniPrimary (citable) accession number: Q59098
Secondary accession number(s): Q0KBW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 121 of the entry and version 2 of the sequence. See 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

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