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Q8NX76

- ODP2_STAAW

UniProt

Q8NX76 - ODP2_STAAW

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene
pdhC, MW0978
Organism
Staphylococcus aureus (strain MW2)
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 – 4011 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

Enzyme and pathway databases

BioCyciSAUR196620:GJ9Z-1002-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
Ordered Locus Names:MW0978
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000418: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162293Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi196620.MW0978.

Structurei

3D structure databases

ProteinModelPortaliQ8NX76.
SMRiQ8NX76. Positions 2-79, 121-165, 187-428.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
KOiK00627.
OMAiVAFRTRI.
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.

Q8NX76-1 [UniParc]FASTAAdd to Basket

« Hide

MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS    50
PVSGTVEEVM VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA 100
KEEAPAEQAP VATQTEEVDE NRTVKAMPSV RKYAREKGVN IKAVSGSGKN 150
GRITKEDVDA YLNGGAPTAS NESAASATSE EVAETPAAPA AVTLEGDFPE 200
TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH RKKFKEIAAE 250
QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT 300
DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN 350
IGSAGGQWFT PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD 400
HRQIDGATGQ NAMNHIKRLL NNPELLLMEG 430
Length:430
Mass (Da):46,382
Last modified:October 1, 2002 - v1
Checksum:i4507074CAE5B7DCF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000033 Genomic DNA. Translation: BAB94843.1.
RefSeqiNP_645795.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94843; BAB94843; BAB94843.
GeneIDi1003090.
KEGGisam:MW0978.
PATRICi19568536. VBIStaAur44266_1027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000033 Genomic DNA. Translation: BAB94843.1 .
RefSeqi NP_645795.1. NC_003923.1.

3D structure databases

ProteinModelPortali Q8NX76.
SMRi Q8NX76. Positions 2-79, 121-165, 187-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196620.MW0978.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB94843 ; BAB94843 ; BAB94843 .
GeneIDi 1003090.
KEGGi sam:MW0978.
PATRICi 19568536. VBIStaAur44266_1027.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281564.
KOi K00627.
OMAi VAFRTRI.
OrthoDBi EOG610413.

Enzyme and pathway databases

BioCyci SAUR196620:GJ9Z-1002-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MW2.

Entry informationi

Entry nameiODP2_STAAW
AccessioniPrimary (citable) accession number: Q8NX76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 78 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

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