PDP1_BOVIN
ID PDP1_BOVIN Reviewed; 538 AA.
AC P35816;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
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=PDP, PPM2C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8396421; DOI=10.1021/bi00086a002;
RA Lawson J.E., Niu X.-D., Browning K.S., Trong H.L., Yan J., Reed L.J.;
RT "Molecular cloning and expression of the catalytic subunit of bovine
RT pyruvate dehydrogenase phosphatase and sequence similarity with protein
RT phosphatase 2C.";
RL Biochemistry 32:8987-8993(1993).
RN [2]
RP SUBUNIT.
RX PubMed=9395502; DOI=10.1074/jbc.272.50.31625;
RA Lawson J.E., Park S.H., Mattison A.R., Yan J., Reed L.J.;
RT "Cloning, expression, and properties of the regulatory subunit of bovine
RT pyruvate dehydrogenase phosphatase.";
RL J. Biol. Chem. 272:31625-31629(1997).
CC -!- FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation
CC of the alpha subunit of the E1 component of the pyruvate dehydrogenase
CC complex.
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:0000269|PubMed:9395502}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L18966; AAA30697.1; ALT_INIT; mRNA.
DR PIR; A48692; A48692.
DR RefSeq; NP_001193282.1; NM_001206353.1.
DR RefSeq; XP_005215704.1; XM_005215647.3.
DR RefSeq; XP_005215707.1; XM_005215650.3.
DR RefSeq; XP_010810497.1; XM_010812195.2.
DR PDB; 3MQ3; X-ray; 2.80 A; A=72-538.
DR PDB; 6V0T; X-ray; 2.10 A; A=72-538.
DR PDBsum; 3MQ3; -.
DR PDBsum; 6V0T; -.
DR AlphaFoldDB; P35816; -.
DR SMR; P35816; -.
DR STRING; 9913.ENSBTAP00000043214; -.
DR PaxDb; P35816; -.
DR PeptideAtlas; P35816; -.
DR PRIDE; P35816; -.
DR Ensembl; ENSBTAT00000000233; ENSBTAP00000000233; ENSBTAG00000000199.
DR GeneID; 280891; -.
DR KEGG; bta:280891; -.
DR CTD; 54704; -.
DR VEuPathDB; HostDB:ENSBTAG00000000199; -.
DR VGNC; VGNC:32713; PDP1.
DR eggNOG; KOG0700; Eukaryota.
DR GeneTree; ENSGT00940000156368; -.
DR HOGENOM; CLU_021928_0_0_1; -.
DR InParanoid; P35816; -.
DR OrthoDB; 461546at2759; -.
DR BRENDA; 3.1.3.43; 908.
DR EvolutionaryTrace; P35816; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000000199; Expressed in occipital lobe and 103 other tissues.
DR ExpressionAtlas; P35816; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; TAS:UniProtKB.
DR GO; GO:1904184; P:positive regulation of pyruvate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Direct protein sequencing; Hydrolase;
KW Magnesium; Metal-binding; Mitochondrion; Protein phosphatase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..71
FT /note="Mitochondrion"
FT CHAIN 72..538
FT /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT phosphatase 1, mitochondrial"
FT /id="PRO_0000025418"
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 HELIX 82..89
FT /evidence="ECO:0007829|PDB:6V0T"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3MQ3"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 205..222
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 232..253
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6V0T"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6V0T"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 499..504
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:6V0T"
FT STRAND 518..525
FT /evidence="ECO:0007829|PDB:6V0T"
FT HELIX 527..533
FT /evidence="ECO:0007829|PDB:6V0T"
SQ SEQUENCE 538 AA; 61184 MW; 1A1C219AD8C3DAE3 CRC64;
MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSPPYIP QSRPRYTPHP AYATFYRPKE
SWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSVL GFDSNQLPAN
APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
EDGSWSAVTL SNDHNAQNER EVERLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
SIDLQKRVIE SGPDQLNDNE YTKFIPPNYY TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT
HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ