ID A0A4W2EIN0_BOBOX Unreviewed; 563 AA.
AC A0A4W2EIN0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial {ECO:0000256|ARBA:ARBA00040842};
DE EC=3.1.3.43 {ECO:0000256|ARBA:ARBA00038972};
DE AltName: Full=Protein phosphatase 2C {ECO:0000256|ARBA:ARBA00041989};
DE AltName: Full=Pyruvate dehydrogenase phosphatase catalytic subunit 1 {ECO:0000256|ARBA:ARBA00041690};
GN Name=PDP1 {ECO:0000313|Ensembl:ENSBIXP00000032643.1};
OS Bos indicus x Bos taurus (Hybrid cattle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000032643.1, ECO:0000313|Proteomes:UP000314981};
RN [1] {ECO:0000313|Proteomes:UP000314981, ECO:0000313|Proteomes:UP000429181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT "Haplotype-resolved cattle genomes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBIXP00000032643.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mitochondrial enzyme that catalyzes the dephosphorylation and
CC concomitant reactivation of the alpha subunit of the E1 component of
CC the pyruvate dehydrogenase complex (PDC), thereby stimulating the
CC conversion of pyruvate into acetyl-CoA.
CC {ECO:0000256|ARBA:ARBA00043921}.
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 Evidence={ECO:0000256|ARBA:ARBA00043727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12670;
CC Evidence={ECO:0000256|ARBA:ARBA00043727};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC subunit. {ECO:0000256|ARBA:ARBA00038577}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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DR Ensembl; ENSBIXT00000044209.1; ENSBIXP00000032643.1; ENSBIXG00000015240.1.
DR Ensembl; ENSBIXT00005009876.1; ENSBIXP00005029769.1; ENSBIXG00005009795.1.
DR GeneTree; ENSGT00940000156368; -.
DR Proteomes; UP000314981; Chromosome 14.
DR Proteomes; UP000429181; Chromosome 14.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832:SF627; [PYRUVATE DEHYDROGENASE [ACETYL-TRANSFERRING]]-PHOSPHATASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000314981}.
FT DOMAIN 134..550
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 563 AA; 63825 MW; 35678369C1788222 CRC64;
MCVCPGPRRI GIPVRSSSLP LFSDAMPAPT QLFFPLIRNC ELSRIYGTAC YCHHKHLCCS
PPYIPQSRPR YTPHPAYATF YRPKESWWQY TQGRRYASTP QKFYLTPPQV NSILKANEYS
FKVPEFDGKN VSSVLGFDSN QLPANAPIED RRSAATCLQT RGMLLGVFDG HAGCACSQAV
SERLFYYIAV SLLPHETLLE IENAVESGRA LLPILQWHKH PNDYFSKEAS KLYFNSLRTY
WQELIDLNTG ESTDIDVKEA LINAFKRLDN DISLEAQVGD PNSFLNYLVL RVAFSGATAC
VAHVDGVDLH VANTGDSRAM LGVQEEDGSW SAVTLSNDHN AQNEREVERL KLEHPKNEAK
SVVKQDRLLG LLMPFRAFGD VKFKWSIDLQ KRVIESGPDQ LNDNEYTKFI PPNYYTPPYL
TAEPEVTYHR LRPQDKFLVL ATDGLWETMH RQDVVRIVGE YLTGMHHQQP IAVGGYKVTL
GQMHGLLTER RAKMSSVFED QNAATHLIRH AVGNNEFGAV DHERLSKMLS LPEELARMYR
DDITIIVVQF NSHVVGAYQN QEQ
//
