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P52904

- ODPB_PEA

UniProt

P52904 - ODPB_PEA

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Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Gene
N/A
Organism
Pisum sativum (Garden pea)
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 sitei82 – 821Thiamine pyrophosphate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: InterPro
  2. 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, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-B
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919Mitochondrion By similarity
Add
BLAST
Chaini20 – 359340Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020463Add
BLAST

Proteomic databases

PRIDEiP52904.
ProMEXiP52904.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta subunits By similarity.

Protein-protein interaction databases

IntActiP52904. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP52904.
SMRiP52904. Positions 25-347.

Family & Domainsi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
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.

P52904-1 [UniParc]FASTAAdd to Basket

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MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG    50
EEVGEYQGAY KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV 100
VEFMTFNFSM QAIDHIINSA AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ 150
HSHCYASWYG SCPGLKVLVP HSAEDARGLL KAAIRDPDPV VFLENELLYG 200
ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG FALKAAEILE 250
KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT 300
SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH 350
RSVPLAAAA 359
Length:359
Mass (Da):38,793
Last modified:October 1, 1996 - v1
Checksum:i5AFE49F165C13C83
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U56697 mRNA. Translation: AAB01223.1.
PIRiT06532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U56697 mRNA. Translation: AAB01223.1 .
PIRi T06532.

3D structure databases

ProteinModelPortali P52904.
SMRi P52904. Positions 25-347.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P52904. 1 interaction.

Proteomic databases

PRIDEi P52904.
ProMEXi P52904.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
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. Luethy M.H., Miernyk J.A., Randall D.D.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiODPB_PEA
AccessioniPrimary (citable) accession number: P52904
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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