Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial

Gene

Pdp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.

Catalytic activityi

[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi144 – 1441Magnesium 1
Metal bindingi144 – 1441Magnesium 2
Metal bindingi145 – 1451Magnesium 1; via carbonyl oxygen
Metal bindingi418 – 4181Magnesium 2
Metal bindingi516 – 5161Magnesium 1

GO - Molecular functioni

  • [pyruvate dehydrogenase (lipoamide)] phosphatase activity Source: RGD
  • calcium ion binding Source: UniProtKB
  • magnesium-dependent protein serine/threonine phosphatase activity Source: RGD
  • magnesium ion binding Source: RGD
  • protein complex binding Source: RGD
  • protein serine/threonine phosphatase activity Source: RGD

GO - Biological processi

  • positive regulation of catalytic activity Source: RGD
  • protein dephosphorylation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.43. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (EC:3.1.3.43)
Short name:
PDP 1
Alternative name(s):
Protein phosphatase 2C
Pyruvate dehydrogenase phosphatase catalytic subunit 1
Short name:
PDPC 1
Gene namesi
Name:Pdp1
Synonyms:Ppm2c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620393. Pdp1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: RGD
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7171MitochondrionBy similarityAdd
BLAST
Chaini72 – 538467[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrialPRO_0000025420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO88483.
PRIDEiO88483.

PTM databases

iPTMnetiO88483.
PhosphoSiteiO88483.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle.

Interactioni

Subunit structurei

Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit.1 Publication

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062054.

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi82 – 9211Combined sources
Beta strandi94 – 974Combined sources
Turni102 – 1043Combined sources
Beta strandi108 – 11710Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi125 – 13612Combined sources
Beta strandi138 – 14912Combined sources
Helixi150 – 16718Combined sources
Helixi170 – 1778Combined sources
Turni178 – 1803Combined sources
Beta strandi190 – 1923Combined sources
Helixi205 – 22117Combined sources
Helixi232 – 25322Combined sources
Helixi258 – 26912Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi274 – 2807Combined sources
Beta strandi283 – 2919Combined sources
Beta strandi293 – 2997Combined sources
Beta strandi305 – 3095Combined sources
Helixi319 – 3279Combined sources
Helixi331 – 3333Combined sources
Helixi334 – 3374Combined sources
Beta strandi338 – 3436Combined sources
Turni344 – 3463Combined sources
Beta strandi347 – 3515Combined sources
Helixi356 – 3583Combined sources
Helixi362 – 3698Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi400 – 4056Combined sources
Beta strandi410 – 4167Combined sources
Helixi418 – 4214Combined sources
Helixi426 – 43712Combined sources
Helixi478 – 48710Combined sources
Beta strandi518 – 5258Combined sources
Helixi527 – 5359Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PNQX-ray1.81A/B72-538[»]
ProteinModelPortaliO88483.
SMRiO88483. Positions 80-538.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88483.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 525417PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0700. Eukaryota.
COG0631. LUCA.
HOGENOMiHOG000220821.
HOVERGENiHBG008162.
InParanoidiO88483.
PhylomeDBiO88483.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 5 hits.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 3 hits.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O88483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPTQLFFP LVRNCELSRI YGTACYCHHK HLCCSPPYIP QNRLRYTPHP
60 70 80 90 100
AYATFCRPRE NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE
110 120 130 140 150
FDGKNVSSIL GFDSNRLPAN APIEDRRSAT TCLQTRGMLL GVFDGHAGCA
160 170 180 190 200
CSQAVSERLF YYIAVSLLPH ETLLEIENAV ESGRALLPIL QWHKHPNDYF
210 220 230 240 250
SKEASKLYFN GLRTYWQELI DLNTGESADI DVKEALINAF KRLDNDISLE
260 270 280 290 300
AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
310 320 330 340 350
EDGSWSAVTL SNDHNAQNER ELQRLKLEHP KNEAKSVVKQ DRLLGLLMPF
360 370 380 390 400
RAFGDVKFKW SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE
410 420 430 440 450
VTYHRLRPQD KFLVLATDGL WETMHRQDVV RIVGEYLTGM HHQQPIAVGG
460 470 480 490 500
YKVTLGQMHG LLTERRAKMS SVFEDQNAAT HLIRHAVGNN EFGAVDHERL
510 520 530
SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ
Length:538
Mass (Da):61,207
Last modified:November 1, 1998 - v1
Checksum:iD546096229B73564
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062740 mRNA. Translation: AAC40167.1.
UniGeneiRn.31799.

Genome annotation databases

UCSCiRGD:620393. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062740 mRNA. Translation: AAC40167.1.
UniGeneiRn.31799.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PNQX-ray1.81A/B72-538[»]
ProteinModelPortaliO88483.
SMRiO88483. Positions 80-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062054.

PTM databases

iPTMnetiO88483.
PhosphoSiteiO88483.

Proteomic databases

PaxDbiO88483.
PRIDEiO88483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620393. rat.

Organism-specific databases

RGDi620393. Pdp1.

Phylogenomic databases

eggNOGiKOG0700. Eukaryota.
COG0631. LUCA.
HOGENOMiHOG000220821.
HOVERGENiHBG008162.
InParanoidiO88483.
PhylomeDBiO88483.

Enzyme and pathway databases

BRENDAi3.1.3.43. 5301.

Miscellaneous databases

EvolutionaryTraceiO88483.
PROiO88483.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 5 hits.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 3 hits.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation."
    Huang B., Gudi R., Wu P., Harris R.A., Hamilton J., Popov K.M.
    J. Biol. Chem. 273:17680-17688(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications."
    Vassylyev D.G., Symersky J.
    J. Mol. Biol. 370:417-426(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 72-538, COFACTOR, METAL-BINDING SITES, SUBUNIT.

Entry informationi

Entry nameiPDP1_RAT
AccessioniPrimary (citable) accession number: O88483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.