Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Acholeplasma laidlawii
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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)-lipoateCuratedNote: Binds 2 lipoyl cofactors covalently.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei516Sequence 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:pdhC
OrganismiAcholeplasma laidlawii
Taxonomic identifieri2148 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622701 – 544Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42N6-lipoyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei154N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

PRIDEiP35489

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP35489
SMRiP35489
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 76Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST76
Domaini113 – 188Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST76
Domaini242 – 279Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA

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
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
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
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

P35489-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP
60 70 80 90 100
VDGTIVSLGA KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA
110 120 130 140 150
APQVAAPAAS GDIYDFKFAD IGEGIHEGTI LQWNFKVGDK VKEGETLVVV
160 170 180 190 200
ETDKVNAELP SPVDGTILKL GKAEGEVIHV GETVVLIGQN GATLEQAQAP
210 220 230 240 250
KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK VLASPVARKL
260 270 280 290 300
ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS
310 320 330 340 350
VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD
360 370 380 390 400
ALVNFRNEAK GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE
410 420 430 440 450
VYIKKFINLG MAVDTPDGLI VPNIKNADRL SVFELASQVR SLADDTIARK
460 470 480 490 500
ISMDQQTGGT FTITNFGSAG IAFGTPVINY PELAILGIGK IDRKPWVVGN
510 520 530 540
EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL LLLS
Length:544
Mass (Da):57,261
Last modified:June 1, 1994 - v1
Checksum:i81E92D869CFD5424
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81753 Genomic DNA Translation: AAA21909.1
PIRiC42653

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81753 Genomic DNA Translation: AAA21909.1
PIRiC42653

3D structure databases

ProteinModelPortaliP35489
SMRiP35489
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP35489

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA

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
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
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
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiODP2_ACHLA
AccessioniPrimary (citable) accession number: P35489
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 23, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again