ID G3HX30_CRIGR Unreviewed; 538 AA.
AC G3HX30;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 ORFNames=I79_015546 {ECO:0000313|EMBL:EGW11764.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW11764.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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 EMBL; JH000852; EGW11764.1; -; Genomic_DNA.
DR RefSeq; XP_007646585.1; XM_007648395.2.
DR AlphaFoldDB; G3HX30; -.
DR STRING; 10029.G3HX30; -.
DR PaxDb; 10029-XP_007637048-1; -.
DR GeneID; 100761381; -.
DR CTD; 54704; -.
DR eggNOG; KOG0700; Eukaryota.
DR InParanoid; G3HX30; -.
DR OrthoDB; 1131727at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
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}; Pyruvate {ECO:0000313|EMBL:EGW11764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT DOMAIN 109..525
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 538 AA; 61221 MW; BFA54A9905E3F320 CRC64;
MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSPTYIP QNRLRYTPHP AYATFCRPRE
NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNQLPAN
APIEDRRSAA TCSQTRDMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESADI DVKEALINAF
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
EDGSWSAVTL SNDHNAQNER ELERLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
WETMHRQDVV RIVGEYLTGM HQQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT
HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ
//
