ID A0A2A2J9I5_9BILA Unreviewed; 237 AA.
AC A0A2A2J9I5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Serine/threonine-protein phosphatase PGAM5, mitochondrial {ECO:0000256|ARBA:ARBA00039765};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE AltName: Full=Phosphoglycerate mutase family member 5 homolog {ECO:0000256|ARBA:ARBA00042520};
DE AltName: Full=Serine/threonine-protein phosphatase Pgam5, mitochondrial {ECO:0000256|ARBA:ARBA00040722};
GN ORFNames=WR25_12374 {ECO:0000313|EMBL:PAV58438.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV58438.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV58438.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV58438.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:0000256|ARBA:ARBA00001512};
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:0000256|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV58438.1}.
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DR EMBL; LIAE01010581; PAV58432.1; -; Genomic_DNA.
DR EMBL; LIAE01010581; PAV58434.1; -; Genomic_DNA.
DR EMBL; LIAE01010581; PAV58435.1; -; Genomic_DNA.
DR EMBL; LIAE01010581; PAV58438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2J9I5; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; 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; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 237 AA; 27338 MW; 84B81FDAA9E7320F CRC64;
MGFPNAWSVN VDFPRFPFPL VFQTMASKMK IIAGSTVALA TFGLFNDYRN SKSSSRSYFF
GRDALAFSHS KGQYLRFDEY FPRGEWDDNW DFRSPEYLVS RKKYELASES EREQMVKGKT
ATATRNIILI RHGQYQINSP DKFLTQLGGF TTFSKKLQTF INLVYKSVDL CFDFESLWKK
TLLSEKRKVS GREQAELVGK RLATSGIKFD EVVMSTMNRA TETAKIILQQ LPKEQKS
//
