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P35489

- ODP2_ACHLA

UniProt

P35489 - ODP2_ACHLA

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Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Gene
pdhC
Organism
Acholeplasma laidlawii
Status
Reviewed - Annotation score: 3 out of 5 - 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 N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

Binds 2 lipoyl cofactors covalently Reviewed prediction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei516 – 5161 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 544544Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-lipoyllysine By similarity
Modified residuei154 – 1541N6-lipoyllysine By similarity

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP35489.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7575Lipoyl-binding 1
Add
BLAST
Domaini114 – 18774Lipoyl-binding 2
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Repeat

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

Sequencei

Sequence statusi: Complete.

P35489-1 [UniParc]FASTAAdd to Basket

« Hide

MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP    50
VDGTIVSLGA KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA 100
APQVAAPAAS GDIYDFKFAD IGEGIHEGTI LQWNFKVGDK VKEGETLVVV 150
ETDKVNAELP SPVDGTILKL GKAEGEVIHV GETVVLIGQN GATLEQAQAP 200
KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK VLASPVARKL 250
ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS 300
VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD 350
ALVNFRNEAK GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE 400
VYIKKFINLG MAVDTPDGLI VPNIKNADRL SVFELASQVR SLADDTIARK 450
ISMDQQTGGT FTITNFGSAG IAFGTPVINY PELAILGIGK IDRKPWVVGN 500
EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL LLLS 544
Length:544
Mass (Da):57,261
Last modified:June 1, 1994 - v1
Checksum:i81E92D869CFD5424
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81753 Genomic DNA. Translation: AAA21909.1.
PIRiC42653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81753 Genomic DNA. Translation: AAA21909.1 .
PIRi C42653.

3D structure databases

ProteinModelPortali P35489.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii."
    Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.
    J. Bacteriol. 174:1388-1396(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiODP2_ACHLA
AccessioniPrimary (citable) accession number: P35489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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