ID PGAM5_XENTR Reviewed; 278 AA.
AC Q6GL33;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Serine/threonine-protein phosphatase PGAM5, mitochondrial;
DE EC=3.1.3.16;
DE AltName: Full=Phosphoglycerate mutase family member 5;
GN Name=pgam5;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Displays phosphatase activity for serine/threonine residues.
CC Has apparently no phosphoglycerate mutase activity. May be regulator of
CC mitochondrial dynamics (By similarity). May be a central mediator for
CC programmed necrosis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The N-terminal 35 amino acids, including the potential
CC transmembrane alpha-helix, function as a non-cleaved mitochondrial
CC targeting sequence that targets the protein to the cytosolic side of
CC the outer mitochondrial membrane. {ECO:0000250}.
CC -!- PTM: Phosphorylated by the RIPK1/RIPK3 complex under necrotic
CC conditions. This phosphorylation increases PGAM5 phosphatase activity
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; BC074682; AAH74682.1; -; mRNA.
DR RefSeq; NP_001004858.1; NM_001004858.1.
DR AlphaFoldDB; Q6GL33; -.
DR SMR; Q6GL33; -.
DR STRING; 8364.ENSXETP00000037568; -.
DR PaxDb; 8364-ENSXETP00000051391; -.
DR GeneID; 448148; -.
DR KEGG; xtr:448148; -.
DR AGR; Xenbase:XB-GENE-948920; -.
DR CTD; 192111; -.
DR Xenbase; XB-GENE-948920; pgam5.
DR eggNOG; KOG4609; Eukaryota.
DR InParanoid; Q6GL33; -.
DR OrthoDB; 2994603at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR20935; PHOSPHOGLYCERATE MUTASE-RELATED; 1.
DR PANTHER; PTHR20935:SF0; SERINE_THREONINE-PROTEIN PHOSPHATASE PGAM5, MITOCHONDRIAL; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane; Necrosis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..278
FT /note="Serine/threonine-protein phosphatase PGAM5,
FT mitochondrial"
FT /id="PRO_0000288787"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 278 AA; 31211 MW; 67923E297F554639 CRC64;
MYLRKALIAG GSAAAAAAAI LGAAAVGKSK GGPDLDILSV VPAATGQWDR NWDRREPISM
VNLSKINGET GEEELQLHLN KHKPKATRHI FLIRHSQYKQ DGKTDFDRVL TPLGREQADL
TGKRLSSLGF KYNHIVYSTM TRAKETTEII SKYLPDVKKS SSDLLREGAP IRPEPQVCHW
KPDFVYYEDG SRIEAAFRHF IHRADPKQEA DSYEILICHA NVIRYIVCRA LQLPPEAWLR
MFLNNGSISY LVIRPNGNVS LRMLGDSGFM PPEKISRT
//
