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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Status
Reviewed-Annotation score: Annotation score: 3 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) (By similarity).By similarity

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei411 – 4111Sequence 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

BioCyciMCAP340047:GC0H-225-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:pdhC
Synonyms:odp2
Ordered Locus Names:MCAP_0227
OrganismiMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Taxonomic identifieri340047 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000001928 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi340047.MCAP_0227.

Structurei

3D structure databases

ProteinModelPortaliQ49110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
KOiK00627.
OMAiATDTDNG.
OrthoDBiEOG610413.

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

Sequencei

Sequence statusi: Complete.

Q49110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKVKFADIG EGLTEGTVAE VLVKVGDVVK EGQSLYFVET DKVNSEIPAP
60 70 80 90 100
VAGKIAVINI KAGQEIKVGD VVMEIEDGSD TSATSEPKAE TKSEAKVEVV
110 120 130 140 150
EENASVVGAT PVSNDVIVRK QTTTVNKSST IKATPLARKV AADLNIDLSL
160 170 180 190 200
VTPTGPNQRI LVADIKNHQA SSTQLASQPI SQPAPTPSPS AHQTIAPTIK
210 220 230 240 250
VVEPSAPLSW DEVPMNGVRK ATVKAMTKSH TEIAAFTGMK NTDITETHKM
260 270 280 290 300
RTELKDHAAA SGIKLTYLAF IIKAVAKSLR DMPNINVRGD FANNKIQFMH
310 320 330 340 350
NINIGIAVDT PNGLMVPVIK GADHLSVFEI AIKISELANK AKDGKLTRAE
360 370 380 390 400
MTEATFTVSN FGSVGLDYAT PIINSPESAI LGVGTMSQTP LYINGELQKR
410 420 430
FIMPLSMTCD HRIIDGADAG RFLIKVQDYL SKPVLLFM
Length:438
Mass (Da):46,927
Last modified:November 1, 1996 - v1
Checksum:i4BF83B697480B4AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62057 Genomic DNA. Translation: AAC44344.1.
CP000123 Genomic DNA. Translation: ABC01559.1.
RefSeqiWP_011387115.1. NC_007633.1.
YP_424214.1. NC_007633.1.

Genome annotation databases

EnsemblBacteriaiABC01559; ABC01559; MCAP_0227.
KEGGimcp:MCAP_0227.
PATRICi20004919. VBIMycCap130493_0230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62057 Genomic DNA. Translation: AAC44344.1.
CP000123 Genomic DNA. Translation: ABC01559.1.
RefSeqiWP_011387115.1. NC_007633.1.
YP_424214.1. NC_007633.1.

3D structure databases

ProteinModelPortaliQ49110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi340047.MCAP_0227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC01559; ABC01559; MCAP_0227.
KEGGimcp:MCAP_0227.
PATRICi20004919. VBIMycCap130493_0230.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
KOiK00627.
OMAiATDTDNG.
OrthoDBiEOG610413.

Enzyme and pathway databases

BioCyciMCAP340047:GC0H-225-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.
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. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in Mycoplasma capricolum."
    Zhu P.P., Peterkofsky A.
    Protein Sci. 5:1719-1736(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: California kid / ATCC 27343 / NCTC 10154.

Entry informationi

Entry nameiODP2_MYCCT
AccessioniPrimary (citable) accession number: Q49110
Secondary accession number(s): Q2SSP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 101 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

Complete 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.