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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 4 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

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei399 – 3991Sequence 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

BRENDAi2.3.1.12. 623.

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
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 428427Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysinePROSITE-ProRule annotation1 Publication

Interactioni

Subunit structurei

Forms a 60-polypeptide structural core with icosahedral symmetry.

Protein-protein interaction databases

DIPiDIP-6156N.
IntActiP11961. 2 interactions.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Beta strandi16 – 216Combined sources
Beta strandi37 – 404Combined sources
Beta strandi45 – 484Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 675Combined sources
Beta strandi69 – 713Combined sources
Helixi133 – 1419Combined sources
Turni146 – 1483Combined sources
Helixi154 – 1563Combined sources
Helixi160 – 1678Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B5SX-ray4.40A/B/C/D/E185-426[»]
1EBDX-ray2.60C130-170[»]
1LABNMR-A2-81[»]
1LACNMR-A2-81[»]
1W3DNMR-A119-171[»]
1W4ENMR-A126-170[»]
1W4FNMR-A126-170[»]
1W4GNMR-A126-170[»]
1W85X-ray2.00I/J123-171[»]
1W88X-ray2.30I/J123-171[»]
2PDDNMR-A129-171[»]
2PDENMR-A129-171[»]
3DUFX-ray2.50I/J1-428[»]
3DV0X-ray2.50I/J1-428[»]
3DVAX-ray2.35I/J1-428[»]
ProteinModelPortaliP11961.
SMRiP11961. Positions 2-81, 126-170, 185-426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11961.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7776Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 17143E1/E3 bindingAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS
60 70 80 90 100
PVKGKVLEIL VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT
110 120 130 140 150
ETVSKEEKVD AVAPNAPAAE AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ
160 170 180 190 200
GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE KAAPAAAKPA TTEGEFPETR
210 220 230 240 250
EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK KFKAIAAEKG
260 270 280 290 300
IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR
310 320 330 340 350
GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG
360 370 380 390 400
SAGGQWFTPV INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR
410 420
MIDGATAQKA LNHIKRLLSD PELLLMEA
Length:428
Mass (Da):46,326
Last modified:January 23, 2007 - v3
Checksum:i2600CD150261ACB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37630.1.
PIRiS10799. S14426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37630.1.
PIRiS10799. S14426.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B5SX-ray4.40A/B/C/D/E185-426[»]
1EBDX-ray2.60C130-170[»]
1LABNMR-A2-81[»]
1LACNMR-A2-81[»]
1W3DNMR-A119-171[»]
1W4ENMR-A126-170[»]
1W4FNMR-A126-170[»]
1W4GNMR-A126-170[»]
1W85X-ray2.00I/J123-171[»]
1W88X-ray2.30I/J123-171[»]
2PDDNMR-A129-171[»]
2PDENMR-A129-171[»]
3DUFX-ray2.50I/J1-428[»]
3DV0X-ray2.50I/J1-428[»]
3DVAX-ray2.35I/J1-428[»]
ProteinModelPortaliP11961.
SMRiP11961. Positions 2-81, 126-170, 185-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6156N.
IntActiP11961. 2 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.3.1.12. 623.

Miscellaneous databases

EvolutionaryTraceiP11961.

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

  1. "Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
    Hawkins C.F., Borges A., Perham R.N.
    Eur. J. Biochem. 191:337-346(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
  2. "Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus."
    Packman L.C., Borges A., Perham R.N.
    Biochem. J. 252:79-86(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-201.
  3. "Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex."
    Dardel F., Laue E.D., Perham R.N.
    Eur. J. Biochem. 201:203-209(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-86.
  4. "Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex."
    Dardel F., Davis A.L., Laue E.D., Perham R.N.
    J. Mol. Biol. 229:1037-1048(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-86, LIPOYLATION AT LYS-43.
  5. "The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
    Kalia Y.N., Brocklehurst S.M., Hipps D.S., Appella E., Sakaguchi K., Perham R.N.
    J. Mol. Biol. 230:323-341(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 129-171.
  6. "Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase."
    Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.
    Structure 4:277-286(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 129-171.

Entry informationi

Entry nameiODP2_GEOSE
AccessioniPrimary (citable) accession number: P11961
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.