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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Thiamine pyrophosphateBy 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 – 1919MitochondrionBy similarityAdd
BLAST
Chaini20 – 359340Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020463Add
BLAST

Proteomic databases

PRIDEiP52904.

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.
ModBaseiSearch...
MobiDBiSearch...

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

« Hide

        10         20         30         40         50
MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG
60 70 80 90 100
EEVGEYQGAY KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV
110 120 130 140 150
VEFMTFNFSM QAIDHIINSA AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ
160 170 180 190 200
HSHCYASWYG SCPGLKVLVP HSAEDARGLL KAAIRDPDPV VFLENELLYG
210 220 230 240 250
ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG FALKAAEILE
260 270 280 290 300
KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT
310 320 330 340 350
SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH

RSVPLAAAA
Length:359
Mass (Da):38,793
Last modified:October 1, 1996 - v1
Checksum:i5AFE49F165C13C83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56697 mRNA. Translation: AAB01223.1.
PIRiT06532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56697 mRNA. Translation: AAB01223.1.
PIRiT06532.

3D structure databases

ProteinModelPortaliP52904.
SMRiP52904. Positions 25-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52904. 1 interaction.

Chemistry

ChEMBLiCHEMBL2366571.

Proteomic databases

PRIDEiP52904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

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: January 7, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.