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
//