ID   PGAM5_CAEEL             Reviewed;         284 AA.
AC   Q09422;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Serine/threonine-protein phosphatase Pgam5, mitochondrial;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q96HS1};
DE   AltName: Full=Phosphoglycerate mutase family member 5 homolog;
GN   Name=pgam-5; ORFNames=R07G3.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   INTERACTION WITH SNK-1.
RX   PubMed=23040073; DOI=10.1016/j.cmet.2012.09.007;
RA   Paek J., Lo J.Y., Narasimhan S.D., Nguyen T.N., Glover-Cutter K.,
RA   Robida-Stubbs S., Suzuki T., Yamamoto M., Blackwell T.K., Curran S.P.;
RT   "Mitochondrial SKN-1/Nrf mediates a conserved starvation response.";
RL   Cell Metab. 16:526-537(2012).
CC   -!- FUNCTION: Displays phosphatase activity for serine/threonine residues.
CC       Has apparently no phosphoglycerate mutase activity.
CC       {ECO:0000250|UniProtKB:Q96HS1}.
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         Evidence={ECO:0000250|UniProtKB:Q96HS1};
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         Evidence={ECO:0000250|UniProtKB:Q96HS1};
CC   -!- SUBUNIT: Interacts with skn-1 isoforms a and c.
CC       {ECO:0000269|PubMed:23040073}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q96HS1}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000305}.
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DR   EMBL; BX284602; CCD70516.1; -; Genomic_DNA.
DR   PIR; T16702; T16702.
DR   RefSeq; NP_495593.2; NM_063192.4.
DR   AlphaFoldDB; Q09422; -.
DR   SMR; Q09422; -.
DR   BioGRID; 39565; 2.
DR   IntAct; Q09422; 1.
DR   STRING; 6239.R07G3.5; -.
DR   EPD; Q09422; -.
DR   PaxDb; Q09422; -.
DR   PeptideAtlas; Q09422; -.
DR   EnsemblMetazoa; R07G3.5.1; R07G3.5.1; WBGene00019941.
DR   GeneID; 174231; -.
DR   KEGG; cel:CELE_R07G3.5; -.
DR   UCSC; R07G3.5; c. elegans.
DR   CTD; 174231; -.
DR   WormBase; R07G3.5; CE31979; WBGene00019941; pgam-5.
DR   eggNOG; KOG4609; Eukaryota.
DR   GeneTree; ENSGT00390000004796; -.
DR   HOGENOM; CLU_063130_1_1_1; -.
DR   InParanoid; Q09422; -.
DR   OMA; WHSPLPR; -.
DR   OrthoDB; 1112626at2759; -.
DR   PhylomeDB; Q09422; -.
DR   Reactome; R-CEL-8934903; Receptor Mediated Mitophagy.
DR   PRO; PR:Q09422; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00019941; Expressed in germ line (C elegans) and 4 other tissues.
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:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..284
FT                   /note="Serine/threonine-protein phosphatase Pgam5,
FT                   mitochondrial"
FT                   /id="PRO_0000065425"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   284 AA;  32490 MW;  820D56CE79E71F90 CRC64;
     MVSKIIKLGV PTATLAVGTL LLGDDEKRSA FFRTASAFTQ NHGHKTFDEH FPRGEWDKNW
     DFRDPISLVD KGKWEKADEE GKKKLIEEKK ATATRNIFLI RHGQYHLDHE VKMLTPLGRE
     QAELLGKRLA NSDIKFTNMT MSTMVRATET ANIILKHLPD DLTRTSSPFI EEGPPYPPVP
     DHKTWRPLDP EFYTEAARIE SAYRKIFHRA SPSQKEDSFE LIVCHANVIR YFICRALQFP
     PEGWLRMSLG NCSLTWITIR PKGHVSVRSI GDIGHLPPNK ISFT