SubmitCancel

Skip Header

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

P11961

- ODP2_GEOSE

UniProt

P11961 - ODP2_GEOSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene
pdhC
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - 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

Binds 1 lipoyl cofactor covalently.

Sites

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

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

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-lipoyllysine

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 – 123
Beta strandi16 – 216
Beta strandi37 – 404
Beta strandi45 – 484
Beta strandi59 – 613
Beta strandi63 – 675
Beta strandi69 – 713
Helixi133 – 1419
Turni146 – 1483
Helixi154 – 1563
Helixi160 – 1678

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP11961.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7675Lipoyl-bindingAdd
BLAST

Region

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

Sequence similaritiesi

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

MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS    50
PVKGKVLEIL VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT 100
ETVSKEEKVD AVAPNAPAAE AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ 150
GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE KAAPAAAKPA TTEGEFPETR 200
EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK KFKAIAAEKG 250
IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR 300
GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG 350
SAGGQWFTPV INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR 400
MIDGATAQKA LNHIKRLLSD PELLLMEA 428
Length:428
Mass (Da):46,326
Last modified:January 23, 2007 - v3
Checksum:i2600CD150261ACB0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53560 Genomic DNA. Translation: CAA37630.1.
PIRiS10799. S14426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53560 Genomic DNA. Translation: CAA37630.1 .
PIRi S10799. S14426.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B5S X-ray 4.40 A/B/C/D/E 185-426 [» ]
1EBD X-ray 2.60 C 130-170 [» ]
1LAB NMR - A 2-81 [» ]
1LAC NMR - A 2-81 [» ]
1W3D NMR - A 119-171 [» ]
1W4E NMR - A 126-170 [» ]
1W4F NMR - A 126-170 [» ]
1W4G NMR - A 126-170 [» ]
1W85 X-ray 2.00 I/J 123-171 [» ]
1W88 X-ray 2.30 I/J 123-171 [» ]
2PDD NMR - A 129-171 [» ]
2PDE NMR - A 129-171 [» ]
3DUF X-ray 2.50 I/J 1-428 [» ]
3DV0 X-ray 2.50 I/J 1-428 [» ]
3DVA X-ray 2.35 I/J 1-428 [» ]
ProteinModelPortali P11961.
SMRi P11961. Positions 2-81, 126-170, 185-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6156N.
IntActi P11961. 2 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P11961.

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

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(1990) [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(1988) [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(1991) [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(1993) [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(1993) [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(1996) [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: September 3, 2014
This is version 112 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