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P65635

- ODP2_STAAM

UniProt

P65635 - ODP2_STAAM

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Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Gene
pdhC, SAV1095
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 3 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 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

BioCyciSAUR158878:GJJ5-1114-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:SAV1095
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162288Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiP65635.

2D gel databases

World-2DPAGE0002:P65635.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi158878.SAV1095.

Structurei

3D structure databases

ProteinModelPortaliP65635.
SMRiP65635. Positions 2-79, 126-160, 187-428.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
KOiK00627.
OMAiEPLKGFH.
OrthoDBiEOG610413.
PhylomeDBiP65635.

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.

P65635-1 [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 AVSLEGDFPE 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):46,368
Last modified:October 11, 2004 - v1
Checksum:i4050074CAE5ACDA4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB57257.1.
RefSeqiNP_371619.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57257; BAB57257; SAV1095.
GeneIDi1121072.
KEGGisav:SAV1095.
PATRICi19562889. VBIStaAur52173_1123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB57257.1 .
RefSeqi NP_371619.1. NC_002758.2.

3D structure databases

ProteinModelPortali P65635.
SMRi P65635. Positions 2-79, 126-160, 187-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158878.SAV1095.

2D gel databases

World-2DPAGE 0002:P65635.

Proteomic databases

PRIDEi P65635.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB57257 ; BAB57257 ; SAV1095 .
GeneIDi 1121072.
KEGGi sav:SAV1095.
PATRICi 19562889. VBIStaAur52173_1123.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281564.
KOi K00627.
OMAi EPLKGFH.
OrthoDBi EOG610413.
PhylomeDBi P65635.

Enzyme and pathway databases

BioCyci SAUR158878:GJJ5-1114-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: Mu50 / ATCC 700699.

Entry informationi

Entry nameiODP2_STAAM
AccessioniPrimary (citable) accession number: P65635
Secondary accession number(s): Q99V06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 68 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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