ID   PGAM5_DROYA             Reviewed;         289 AA.
AC   B4PY69;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Serine/threonine-protein phosphatase Pgam5, mitochondrial {ECO:0000250|UniProtKB:O46084};
DE            EC=3.1.3.16;
DE   AltName: Full=Phosphoglycerate mutase family member 5 homolog {ECO:0000250|UniProtKB:O46084};
GN   Name=Pgam5 {ECO:0000250|UniProtKB:O46084}; ORFNames=GE16503;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDX00942.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDX00942.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Displays phosphatase activity for serine/threonine residues,
CC       and dephosphorylates and activates Pk92B kinase. Has apparently no
CC       phosphoglycerate mutase activity (By similarity).
CC       {ECO:0000250|UniProtKB:O46084}.
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   -!- SUBUNIT: Interacts with Pk92B/ASK1. {ECO:0000250|UniProtKB:O46084}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:O46084}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000255}.
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DR   EMBL; CM000162; EDX00942.1; -; Genomic_DNA.
DR   RefSeq; XP_002099834.1; XM_002099798.2.
DR   AlphaFoldDB; B4PY69; -.
DR   SMR; B4PY69; -.
DR   EnsemblMetazoa; FBtr0263021; FBpp0261513; FBgn0234020.
DR   GeneID; 6523962; -.
DR   eggNOG; KOG4609; Eukaryota.
DR   HOGENOM; CLU_063130_0_1_1; -.
DR   OMA; QLPLFAW; -.
DR   OrthoDB; 2994603at2759; -.
DR   PhylomeDB; B4PY69; -.
DR   Proteomes; UP000002282; Chromosome X.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019900; F:kinase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:EnsemblMetazoa.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IEA:EnsemblMetazoa.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:EnsemblMetazoa.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0072347; P:response to anesthetic; IEA:EnsemblMetazoa.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane.
FT   CHAIN           1..289
FT                   /note="Serine/threonine-protein phosphatase Pgam5,
FT                   mitochondrial"
FT                   /id="PRO_0000390712"
SQ   SEQUENCE   289 AA;  33139 MW;  02BF1E5205DE3728 CRC64;
     MRKLTSFVCG TGAGFAAYYL QRLRDPQAAV HNSWTNSDKP VDPWALWDTN WDCREPRALV
     RPLRNSQPEE ENRYNAELEK AKAKKARHII LVRHGEYLDV GDSDDTHHLT DRGRKQAEFT
     GKRLSELGIK WDKIVASTMV RAQETSDIIL KQIEFEKEKV VNCAFLREGA PIPPQPPVGH
     WKPEASQFLR DGSRIEAAFR RYFHRAYPDQ EKESYTLIVG HGNVIRYFVC RALQFPAEGW
     LRISINHASI TWLTISPSGN VSIKYLGDSG FMPPELLTNR IPRDVKNVV
//