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P35816 (PDP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
Short name=PDP 1
EC=3.1.3.43
Alternative name(s):
Protein phosphatase 2C
Pyruvate dehydrogenase phosphatase catalytic subunit 1
Short name=PDPC 1
Gene names
Name:PDP1
Synonyms:PDP, PPM2C
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Subunit structure

Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit. Ref.2

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the PP2C family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7171Mitochondrion
Chain72 – 538467[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
PRO_0000025418

Sites

Metal binding1441Magnesium 1 By similarity
Metal binding1441Magnesium 2 By similarity
Metal binding1451Magnesium 1; via carbonyl oxygen By similarity
Metal binding4181Magnesium 2 By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine By similarity

Secondary structure

1 ............................................................. 538
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35816 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 1A1C219AD8C3DAE3

FASTA53861,184
        10         20         30         40         50         60 
MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSPPYIP QSRPRYTPHP AYATFYRPKE 

        70         80         90        100        110        120 
SWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSVL GFDSNQLPAN 

       130        140        150        160        170        180 
APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV 

       190        200        210        220        230        240 
ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF 

       250        260        270        280        290        300 
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE 

       310        320        330        340        350        360 
EDGSWSAVTL SNDHNAQNER EVERLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW 

       370        380        390        400        410        420 
SIDLQKRVIE SGPDQLNDNE YTKFIPPNYY TPPYLTAEPE VTYHRLRPQD KFLVLATDGL 

       430        440        450        460        470        480 
WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT 

       490        500        510        520        530 
HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ

« Hide

References

[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: 8396421] [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: 9395502] [Abstract]
Cited for: SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L18966 mRNA. Translation: AAA30697.1. Different initiation.
IPIIPI00837836.
PIRA48692.
RefSeqNP_001193282.1. NM_001206353.1.
UniGeneBt.3889.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MQ3X-ray2.80A72-538[»]
3N3CX-ray2.10A72-538[»]
ProteinModelPortalP35816.
SMRP35816. Positions 80-538.
ModBaseSearch...

Protein-protein interaction databases

STRINGP35816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000233; ENSBTAP00000000233; ENSBTAG00000000199.
GeneID280891.
KEGGbta:280891.

Organism-specific databases

CTD54704.

Phylogenomic databases

eggNOGmaNOG08166.
GeneTreeENSGT00390000006874.
HOVERGENHBG008162.
InParanoidP35816.
OrthoDBEOG4XD3QP.
PhylomeDBP35816.

Family and domain databases

InterProIPR001932. PP2C-like.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
Gene3DG3DSA:3.60.40.10. PP2C-related. 3 hits.
KOK01102.
PANTHERPTHR13832. PP2C. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. PP2C-related. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDP1_BOVIN
AccessionPrimary (citable) accession number: P35816
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 16, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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