ID G1QRM9_NOMLE Unreviewed; 596 AA.
AC G1QRM9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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:ENSNLEP00000003597.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000003597.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000003597.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000003597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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; ADFV01043040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003268358.3; XM_003268310.3.
DR AlphaFoldDB; G1QRM9; -.
DR STRING; 61853.ENSNLEP00000003597; -.
DR Ensembl; ENSNLET00000003772.3; ENSNLEP00000003597.1; ENSNLEG00000002967.3.
DR GeneID; 100598000; -.
DR KEGG; nle:100598000; -.
DR CTD; 54704; -.
DR eggNOG; KOG0700; Eukaryota.
DR GeneTree; ENSGT00940000156368; -.
DR HOGENOM; CLU_021928_0_0_1; -.
DR InParanoid; G1QRM9; -.
DR OMA; DVRTPPY; -.
DR OrthoDB; 1131727at2759; -.
DR TreeFam; TF313505; -.
DR Proteomes; UP000001073; Chromosome 16.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004741; F:[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UP000001073}.
FT DOMAIN 168..584
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 596 AA; 67449 MW; 4D403E6C738DAF08 CRC64;
MSISALLSMG RCCCRCCCPR GLWMLSAPCC DDRRMCVCPG PRRIGIPVRS SSLPLFSDAM
PAPTQLFFPL IRNCELSRIY GTACYCHHKH LCCSSSYIPQ SRLRYTPHPA YATFCRPKEN
WWQYTQGRRY ASTPQKFYLT PPQVNSILKA NEYSFKVPEF DGKNVSSILG FDSNQLPANA
PIEDRRSAAT CLQTRGMLLG VFDGHAGCAC SQAVSERLFY YIAVSLLPHE TLLEIENAVE
SGRALLPILQ WHKHPNDYFS KEASKLYFNS LRTYWQELID LNTGESTDID VKEALINAFK
RLDSDISLEA QVGDPNSFLN YLVLRVAFSG ATACVAHVDG VDLHVANTGD SRAMLGVQEE
DGSWSAVTLS NDHNAQNERE LERLKLEHPK SEAKSVVKQD RLLGLLMPFR AFGDVKFKWS
IDLQKRVIES GPDQLNDNEY TKFIPPNYHT PPYLTAEPEV TYHRLRPQDK FLVLATDGLW
ETMHRQDVVR IVGEYLTGMH HQQPIAVGGY KVTLGQMHGL LTERRTKMSS VFEDQNAATH
LIRHAVGNNE FGTVDHERLS KMLSLPEELA RMYRDDITII VVQFNSHVVG AYQNQE
//
