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P21874

- ODPB_GEOSE

UniProt

P21874 - ODPB_GEOSE

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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene
pdhB
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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

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

Cofactori

Thiamine pyrophosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphate By 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

Enzyme and pathway databases

SABIO-RKP21874.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Gene namesi
Name:pdhB
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 325324Pyruvate dehydrogenase E1 component subunit betaPRO_0000162221Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

DIPiDIP-29597N.
IntActiP21874. 1 interaction.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Helixi6 – 2015
Beta strandi24 – 285
Beta strandi32 – 343
Turni40 – 434
Helixi44 – 485
Turni50 – 523
Beta strandi53 – 553
Helixi60 – 7213
Beta strandi76 – 805
Helixi84 – 896
Helixi91 – 955
Helixi98 – 1003
Helixi101 – 1044
Turni105 – 1073
Beta strandi114 – 1196
Beta strandi121 – 1233
Turni127 – 1293
Helixi134 – 1374
Beta strandi144 – 1463
Helixi151 – 16313
Beta strandi164 – 1663
Beta strandi168 – 1736
Turni174 – 1763
Beta strandi177 – 1793
Beta strandi181 – 1833
Beta strandi197 – 2004
Beta strandi203 – 2097
Helixi213 – 22614
Beta strandi231 – 2355
Beta strandi237 – 2415
Helixi244 – 25411
Beta strandi257 – 2648
Beta strandi267 – 2693
Helixi270 – 28112
Helixi282 – 2843
Beta strandi290 – 2945
Beta strandi296 – 2994
Helixi302 – 3043
Helixi305 – 3084
Helixi312 – 32312

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W85X-ray2.00B/D/F/H2-325[»]
1W88X-ray2.30B/D/F/H2-325[»]
3DUFX-ray2.50B/D/F/H1-325[»]
3DV0X-ray2.50B/D/F/H1-325[»]
3DVAX-ray2.35B/D/F/H1-325[»]
ProteinModelPortaliP21874.
SMRiP21874. Positions 2-325.

Miscellaneous databases

EvolutionaryTraceiP21874.

Family & Domainsi

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21874-1 [UniParc]FASTAAdd to Basket

« Hide

MAQMTMVQAI TDALRIELKN DPNVLIFGED VGVNGGVFRA TEGLQAEFGE    50
DRVFDTPLAE SGIGGLAIGL ALQGFRPVPE IQFFGFVYEV MDSICGQMAR 100
IRYRTGGRYH MPITIRSPFG GGVHTPELHS DSLEGLVAQQ PGLKVVIPST 150
PYDAKGLLIS AIRDNDPVIF LEHLKLYRSF RQEVPEGEYT IPIGKADIKR 200
EGKDITIIAY GAMVHESLKA AAELEKEGIS AEVVDLRTVQ PLDIETIIGS 250
VEKTGRAIVV QEAQRQAGIA ANVVAEINER AILSLEAPVL RVAAPDTVYP 300
FAQAESVWLP NFKDVIETAK KVMNF 325
Length:325
Mass (Da):35,460
Last modified:January 23, 2007 - v2
Checksum:iAD1F2D4F82D652AC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53560 Genomic DNA. Translation: CAA37629.1.
PIRiS14230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53560 Genomic DNA. Translation: CAA37629.1 .
PIRi S14230.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W85 X-ray 2.00 B/D/F/H 2-325 [» ]
1W88 X-ray 2.30 B/D/F/H 2-325 [» ]
3DUF X-ray 2.50 B/D/F/H 1-325 [» ]
3DV0 X-ray 2.50 B/D/F/H 1-325 [» ]
3DVA X-ray 2.35 B/D/F/H 1-325 [» ]
ProteinModelPortali P21874.
SMRi P21874. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29597N.
IntActi P21874. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P21874.

Miscellaneous databases

EvolutionaryTracei P21874.

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. "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], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
  2. "Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
    Borges A., Hawkins C.F., Packman L.C., Perham R.N.
    Eur. J. Biochem. 194:95-102(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiODPB_GEOSE
AccessioniPrimary (citable) accession number: P21874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 90 of the entry and version 2 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

External Data

Dasty 3

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