ID   PGAM5_DROPS             Reviewed;         289 AA.
AC   Q29HG0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Serine/threonine-protein phosphatase Pgam5, mitochondrial;
DE            EC=3.1.3.16;
DE   AltName: Full=Phosphoglycerate mutase family member 5 homolog;
GN   Name=Pgam5; ORFNames=GA13269;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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). {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   -!- SUBUNIT: Interacts with Pk92B/ASK1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000305}.
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DR   EMBL; CH379064; EAL31798.1; -; Genomic_DNA.
DR   RefSeq; XP_001354743.1; XM_001354707.3.
DR   AlphaFoldDB; Q29HG0; -.
DR   SMR; Q29HG0; -.
DR   STRING; 46245.Q29HG0; -.
DR   EnsemblMetazoa; FBtr0284485; FBpp0282923; FBgn0073306.
DR   GeneID; 4815173; -.
DR   KEGG; dpo:4815173; -.
DR   eggNOG; KOG4609; Eukaryota.
DR   HOGENOM; CLU_063130_0_1_1; -.
DR   InParanoid; Q29HG0; -.
DR   OMA; SWVSIYP; -.
DR   PhylomeDB; Q29HG0; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0073306; Expressed in female reproductive system and 3 other cell types or tissues.
DR   ExpressionAtlas; Q29HG0; baseline.
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;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..289
FT                   /note="Serine/threonine-protein phosphatase Pgam5,
FT                   mitochondrial"
FT                   /id="PRO_0000288790"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   289 AA;  33069 MW;  7F67EB09A3BFC81B CRC64;
     MRKFTAFACG TGAGLLTFYL TKLNEPKAAV HNSWTRSEKP VDPCALWDHN WDLRDPKSLV
     KPVKNDLSQE QNRYNSELEK VVPKHARHII LIRHGEYLDV GDTDETHHLT ERGREQAKYT
     GKRLCELGIK WDKVIASTMV RAQETADIIL NEIDYEKAKV KNCAFLREGA PIPPQPPVGH
     WKPEASQFFR DGARIEAAFR RYFYRAYPDQ TKDSYTLLVG HGNVIRYFVC RALQFPPEAW
     LRISINHASI TWLTISPSGN VSIKYLGDTG FMPVNHLTNR IPRAAKNVV
//