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
Bos taurus (Bovine)
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+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  • dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.43. 908.
ReactomeiR-BTA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.

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:PDP, PPM2C
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7171MitochondrionAdd
BLAST
Chaini72 – 538467[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrialPRO_0000025418Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP35816.
PRIDEiP35816.

Expressioni

Gene expression databases

ExpressionAtlasiP35816. baseline.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000043214.

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 895Combined sources
Turni90 – 923Combined sources
Beta strandi94 – 974Combined sources
Beta strandi107 – 11711Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi125 – 13612Combined sources
Beta strandi138 – 14912Combined sources
Helixi150 – 16617Combined sources
Helixi170 – 1789Combined sources
Beta strandi190 – 1923Combined sources
Helixi205 – 22016Combined 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 – 3106Combined sources
Helixi319 – 3279Combined sources
Helixi331 – 3333Combined sources
Turni334 – 3363Combined sources
Beta strandi337 – 3393Combined sources
Turni344 – 3463Combined sources
Beta strandi347 – 3515Combined sources
Helixi356 – 3583Combined sources
Helixi362 – 3687Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi400 – 4056Combined sources
Beta strandi410 – 4167Combined sources
Helixi418 – 4214Combined sources
Helixi426 – 43712Combined sources
Helixi478 – 4869Combined sources
Helixi511 – 5144Combined sources
Beta strandi518 – 5258Combined sources
Helixi527 – 5337Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MQ3X-ray2.80A72-538[»]
3N3CX-ray2.10A72-538[»]
ProteinModelPortaliP35816.
SMRiP35816. Positions 80-538.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35816.

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.
GeneTreeiENSGT00390000006874.
HOGENOMiHOG000220821.
HOVERGENiHBG008162.
InParanoidiP35816.
KOiK01102.

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.

P35816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSPPYIP QSRPRYTPHP
60 70 80 90 100
AYATFYRPKE SWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE
110 120 130 140 150
FDGKNVSSVL GFDSNQLPAN APIEDRRSAA TCLQTRGMLL GVFDGHAGCA
160 170 180 190 200
CSQAVSERLF YYIAVSLLPH ETLLEIENAV ESGRALLPIL QWHKHPNDYF
210 220 230 240 250
SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF KRLDNDISLE
260 270 280 290 300
AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
310 320 330 340 350
EDGSWSAVTL SNDHNAQNER EVERLKLEHP KNEAKSVVKQ DRLLGLLMPF
360 370 380 390 400
RAFGDVKFKW SIDLQKRVIE SGPDQLNDNE YTKFIPPNYY 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):61,184
Last modified:June 1, 1994 - v1
Checksum:i1A1C219AD8C3DAE3
GO

Sequence cautioni

The sequence AAA30697.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18966 mRNA. Translation: AAA30697.1. Different initiation.
PIRiA48692.
RefSeqiNP_001193282.1. NM_001206353.1.
XP_005215704.1. XM_005215647.3.
XP_005215707.1. XM_005215650.3.
XP_010810497.1. XM_010812195.2.
UniGeneiBt.3889.

Genome annotation databases

EnsembliENSBTAT00000000233; ENSBTAP00000000233; ENSBTAG00000000199.
GeneIDi280891.
KEGGibta:280891.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18966 mRNA. Translation: AAA30697.1. Different initiation.
PIRiA48692.
RefSeqiNP_001193282.1. NM_001206353.1.
XP_005215704.1. XM_005215647.3.
XP_005215707.1. XM_005215650.3.
XP_010810497.1. XM_010812195.2.
UniGeneiBt.3889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MQ3X-ray2.80A72-538[»]
3N3CX-ray2.10A72-538[»]
ProteinModelPortaliP35816.
SMRiP35816. Positions 80-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000043214.

Proteomic databases

PaxDbiP35816.
PRIDEiP35816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000233; ENSBTAP00000000233; ENSBTAG00000000199.
GeneIDi280891.
KEGGibta:280891.

Organism-specific databases

CTDi54704.

Phylogenomic databases

eggNOGiKOG0700. Eukaryota.
COG0631. LUCA.
GeneTreeiENSGT00390000006874.
HOGENOMiHOG000220821.
HOVERGENiHBG008162.
InParanoidiP35816.
KOiK01102.

Enzyme and pathway databases

BRENDAi3.1.3.43. 908.
ReactomeiR-BTA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

EvolutionaryTraceiP35816.
NextBioi20805025.

Gene expression databases

ExpressionAtlasiP35816. baseline.

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. "Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C."
    Lawson J.E., Niu X.-D., Browning K.S., Trong H.L., Yan J., Reed L.J.
    Biochemistry 32:8987-8993(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase."
    Lawson J.E., Park S.H., Mattison A.R., Yan J., Reed L.J.
    J. Biol. Chem. 272:31625-31629(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiPDP1_BOVIN
AccessioniPrimary (citable) accession number: P35816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 11, 2016
This is version 122 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, Direct protein sequencing, 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.