PDP1_PONAB
ID PDP1_PONAB Reviewed; 537 AA.
AC Q5RA52; Q5R471; Q5R4P7; Q5R968;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial;
DE Short=PDP 1;
DE EC=3.1.3.43;
DE AltName: Full=Protein phosphatase 2C;
DE AltName: Full=Pyruvate dehydrogenase phosphatase catalytic subunit 1;
DE Short=PDPC 1;
DE Flags: Precursor;
GN Name=PDP1; Synonyms=PPM2C;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation
CC of the alpha subunit of the E1 component of the pyruvate dehydrogenase
CC complex. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha
CC subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] +
CC phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-
CC COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.43;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH93269.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH93445.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR859169; CAH91358.1; -; mRNA.
DR EMBL; CR859524; CAH91692.1; -; mRNA.
DR EMBL; CR861198; CAH93269.1; ALT_INIT; mRNA.
DR EMBL; CR861387; CAH93445.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001127016.1; NM_001133544.1.
DR RefSeq; NP_001128828.1; NM_001135356.1.
DR AlphaFoldDB; Q5RA52; -.
DR SMR; Q5RA52; -.
DR STRING; 9601.ENSPPYP00000021027; -.
DR Ensembl; ENSPPYT00000051421; ENSPPYP00000045426; ENSPPYG00000018747.
DR GeneID; 100174041; -.
DR KEGG; pon:100174041; -.
DR CTD; 54704; -.
DR eggNOG; KOG0700; Eukaryota.
DR GeneTree; ENSGT00940000156368; -.
DR HOGENOM; CLU_021928_0_0_1; -.
DR InParanoid; Q5RA52; -.
DR OrthoDB; 461546at2759; -.
DR TreeFam; TF313505; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Hydrolase; Magnesium; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..71
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 72..537
FT /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT phosphatase 1, mitochondrial"
FT /id="PRO_0000341945"
FT DOMAIN 109..525
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J1"
FT CONFLICT 250
FT /note="E -> G (in Ref. 1; CAH93445)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="K -> E (in Ref. 1; CAH91692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 61077 MW; 07AE822466FE4DF0 CRC64;
MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSSSYIP QSRLRYTPHP AYATFCRPKE
NWWHYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNQLPAN
APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
EDGSWSALTL SNDHNAQNER ELERLKLEHP KSEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRTKMS SVFEDQNAAT
HLIRHAVGNN EFGTVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQE
