PGAM5_DROER
ID PGAM5_DROER Reviewed; 289 AA.
AC B3P9N0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=GG12675;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV45526.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV45526.1};
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, ECO:0000255}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255}.
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DR EMBL; CH954183; EDV45526.1; -; Genomic_DNA.
DR RefSeq; XP_001982557.1; XM_001982521.2.
DR AlphaFoldDB; B3P9N0; -.
DR SMR; B3P9N0; -.
DR STRING; 7220.FBpp0131221; -.
DR EnsemblMetazoa; FBtr0132729; FBpp0131221; FBgn0104963.
DR GeneID; 6555713; -.
DR KEGG; der:6555713; -.
DR eggNOG; KOG4609; Eukaryota.
DR HOGENOM; CLU_063130_0_1_1; -.
DR OMA; WHSPLPR; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; B3P9N0; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Serine/threonine-protein phosphatase Pgam5,
FT mitochondrial"
FT /id="PRO_0000390704"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 289 AA; 33151 MW; 324AED21AA10ABB0 CRC64;
MRKLTSFVCG TGAGLAVYYL QRLRDPQATV NNSWTNSEKP VDPWALWDTN WDCREPRALV
RPLRNSQPEE ENRYNAELEK AKAKKARHII LVRHGEYLDV GDSDDTHHLT ERGRKQAEFT
GKRLCELGIK WDKVVASTMV RAQETSDIIL KQIDFEKEKV VNCAFLREGA PIPPQPPVGH
WKPEASQFLR DGSRIEAAFR RYFYRAYPDQ EKESYTLIVG HGNVIRYFVC RALQFPAEGW
LRISINHASI TWLTISPSGN VSIKYLGDSG FMPAELLTHR IPRDAKNVV
