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Q59821

- ODP2_STAAU

UniProt

Q59821 - ODP2_STAAU

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Staphylococcus aureus
Status
Reviewed - 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).

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei401 – 4011Sequence 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

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
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysineBy similarity

Proteomic databases

PRIDEiQ59821.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ59821.
SMRiQ59821. Positions 2-79, 121-165, 187-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.

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.

Q59821-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS
60 70 80 90 100
PVSGTVEEVM VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA
110 120 130 140 150
KEEAPAEQAP VATQTEEVDE NRTVKAMPSV RKYAREKGVN IKAVSGSGKN
160 170 180 190 200
GRITKEDVDA YLNGGAPTAS NESADSATNE EVAETPAAPA AVSLEGDFPE
210 220 230 240 250
TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH RKKFKEIAAE
260 270 280 290 300
QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT
310 320 330 340 350
DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN
360 370 380 390 400
IGSAGGQWFT PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD
410 420 430
HRQIDGATGQ NAMNHIKRLL NNPELLLMEG
Length:430
Mass (Da):46,439
Last modified:November 1, 1996 - v1
Checksum:iAFE00748A65ACDA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58434 Genomic DNA. Translation: CAA41339.1.
PIRiS19722.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58434 Genomic DNA. Translation: CAA41339.1 .
PIRi S19722.

3D structure databases

ProteinModelPortali Q59821.
SMRi Q59821. Positions 2-79, 121-165, 187-428.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q59821.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0508.

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. "Lipoamide dehydrogenase of Staphylococcus aureus: nucleotide sequence and sequence analysis."
    Hemila H.
    Biochim. Biophys. Acta 1129:119-123(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 27733 / V8.

Entry informationi

Entry nameiODP2_STAAU
AccessioniPrimary (citable) accession number: Q59821
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 1, 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3