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P0A0A3

- ODPB_STAAU

UniProt

P0A0A3 - ODPB_STAAU

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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Staphylococcus aureus
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) (By similarity).By similarity

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Gene namesi
Name:pdhB
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Pyruvate dehydrogenase E1 component subunit betaPRO_0000162234Add
BLAST

Proteomic databases

PRIDEiP0A0A3.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

3D structure databases

ProteinModelPortaliP0A0A3.
SMRiP0A0A3. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0022.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A0A3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQMTMVQAI NDALKTELKN DQDVLIFGED VGVNGGVFRV TEGLQKEFGE
60 70 80 90 100
DRVFDTPLAE SGIGGLAMGL AVEGFRPVME VQFLGFVFEV FDAIAGQIAR
110 120 130 140 150
TRFRSGGTKT APVTIRSPFG GGVHTPELHA DNLEGILAQS PGLKVVIPSG
160 170 180 190 200
PYDAKGLLIS SIRSNDPVVY LEHMKLYRSF REEVPEEEYT IDIGKANVKK
210 220 230 240 250
EGNDISIITY GAMVQESMKA AEELEKDGYS VEVIDLRTVQ PIDVDTIVAS
260 270 280 290 300
VEKTGRAVVV QEAQRQAGVG AAVVAELSER AILSLEAPIG RVAAADTIYP
310 320
FTQAENVWLP NKNDIIEKAK ETLEF
Length:325
Mass (Da):35,246
Last modified:March 1, 2005 - v1
Checksum:i432ABDF6E4A720D5
GO

Mass spectrometryi

Molecular mass is 35230 Da from positions 1 - 325. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235026 Genomic DNA. Translation: AAF36410.1.
RefSeqiWP_000068176.1. NZ_JJOP01000033.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235026 Genomic DNA. Translation: AAF36410.1 .
RefSeqi WP_000068176.1. NZ_JJOP01000033.1.

3D structure databases

ProteinModelPortali P0A0A3.
SMRi P0A0A3. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P0A0A3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0022.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Synthesis of pyruvate dehydrogenase is stimulated by osmotic stress in Staphylococcus aureus."
    Vilhelmsson O., Miller K.J.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 12600 / IAM 12544 / NCTC 8532.
  2. "Identification of Staphylococcus aureus proteins recognized by the antibody-mediated immune response to a biofilm infection."
    Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.
    Infect. Immun. 74:3415-3426(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: MRSA-M2.

Entry informationi

Entry nameiODPB_STAAU
AccessioniPrimary (citable) accession number: P0A0A3
Secondary accession number(s): Q9L6H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: November 26, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program