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Protein

Pyruvate dehydrogenase protein X component

Gene

PDHX

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-5362517. Signaling by Retinoic Acid.
R-BTA-70268. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase protein X component
Alternative name(s):
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
E3-binding protein
Short name:
E3BP
proX
Gene namesi
Name:PDHX
Synonyms:PDX1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionBy similarityAdd
BLAST
Chaini54 – 501448Pyruvate dehydrogenase protein X componentPRO_0000162301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-lipoyllysinePROSITE-ProRule annotationBy similarity
Modified residuei194 – 1941N6-acetyllysineBy similarity
Modified residuei394 – 3941N6-succinyllysineBy similarity

Post-translational modificationi

Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP22439.
PeptideAtlasiP22439.
PRIDEiP22439.

Expressioni

Gene expression databases

BgeeiENSBTAG00000018261.

Interactioni

Subunit structurei

Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). Interacts with SIRT4 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024307.

Structurei

3D structure databases

ProteinModelPortaliP22439.
SMRiP22439. Positions 57-144, 174-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13277Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 21432Interaction with DLDAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi149 – 17022Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0557. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00810000125418.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiP22439.
KOiK13997.
OMAiSWRLGCD.
OrthoDBiEOG091G0CAV.
TreeFamiTF332256.

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.

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

P22439-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASWRLGCD PRLLRCLLGF GSRRSPELVK GAARWSVGRG ASWRWFHSTQ
60 70 80 90 100
WLRADPIKIL MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV
110 120 130 140 150
TLDASDDGIL AKIVVAEGSK NIRLGSLIGL LVEEGEDWKH VEIPKDTGPP
160 170 180 190 200
PPAAKPSVPP PSAEPQIATP VKKEHPPGKV QFRLSPAARN ILEKHALDAN
210 220 230 240 250
QGTATGPRGI FTKEDALKLV QLKQTGKITE PRPTAALPTT PAAPLPPQAA
260 270 280 290 300
ATASYPRPMI PPVSTPGQPN VEGTFTEIPA SNIRRVIAKR LTESKSTIPH
310 320 330 340 350
AYATTDCDLG AVLTARQNLV RDDIKVSVND FIIKAAAVTL KQMPNVNASW
360 370 380 390 400
DGEGAKQLPS IDISVAVATD RGLITPVIKD AAAKGLQEIA DSVKALSKKA
410 420 430 440 450
RDGKLLPEEY QGGSFSISNL GMFGIDEFTA VINPPQACIL AVGRFRPVLK
460 470 480 490 500
LTQDEEGNAQ LQQRQLITVT MSSDSRVVDD ELATRFLESF KANLENPLRL

A
Length:501
Mass (Da):53,886
Last modified:June 16, 2009 - v3
Checksum:iA52F1813706AAD5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551D → G AA sequence (PubMed:2914903).Curated
Sequence conflicti78 – 781K → I AA sequence (PubMed:2914903).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661P → G.1 Publication
Natural varianti72 – 721N → G.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120413 mRNA. Translation: AAI20414.1.
PIRiA32040.
RefSeqiNP_001069219.1. NM_001075751.1.
UniGeneiBt.6683.

Genome annotation databases

EnsembliENSBTAT00000024307; ENSBTAP00000024307; ENSBTAG00000018261.
GeneIDi517402.
KEGGibta:517402.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120413 mRNA. Translation: AAI20414.1.
PIRiA32040.
RefSeqiNP_001069219.1. NM_001075751.1.
UniGeneiBt.6683.

3D structure databases

ProteinModelPortaliP22439.
SMRiP22439. Positions 57-144, 174-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024307.

Proteomic databases

PaxDbiP22439.
PeptideAtlasiP22439.
PRIDEiP22439.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024307; ENSBTAP00000024307; ENSBTAG00000018261.
GeneIDi517402.
KEGGibta:517402.

Organism-specific databases

CTDi8050.

Phylogenomic databases

eggNOGiKOG0557. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00810000125418.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiP22439.
KOiK13997.
OMAiSWRLGCD.
OrthoDBiEOG091G0CAV.
TreeFamiTF332256.

Enzyme and pathway databases

ReactomeiR-BTA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-5362517. Signaling by Retinoic Acid.
R-BTA-70268. Pyruvate metabolism.

Gene expression databases

BgeeiENSBTAG00000018261.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiODPX_BOVIN
AccessioniPrimary (citable) accession number: P22439
Secondary accession number(s): Q0P576
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.