ID W2R2Y7_PHYPN Unreviewed; 447 AA.
AC W2R2Y7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=Serine/threonine-protein phosphatase Pgam5, mitochondrial {ECO:0000256|ARBA:ARBA00040722};
GN ORFNames=PPTG_04493 {ECO:0000313|EMBL:ETN19084.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN19084.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN19084.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN19084.1,
RC ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KI669565; ETN19084.1; -; Genomic_DNA.
DR RefSeq; XP_008894983.1; XM_008896735.1.
DR AlphaFoldDB; W2R2Y7; -.
DR STRING; 761204.W2R2Y7; -.
DR EnsemblProtists; ETN19084; ETN19084; PPTG_04493.
DR GeneID; 20174584; -.
DR VEuPathDB; FungiDB:PPTG_04493; -.
DR OrthoDB; 2994603at2759; -.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 Pfam; PF00169; PH; 1.
DR SMART; SM00855; PGAM; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000018817}.
FT DOMAIN 96..193
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 50009 MW; 86AC860A49891D29 CRC64;
MAGPTMEVVS PAQAEDDMRP SHMHNSRLST VNFYTPNSDG LGATQVLGGS QAPRQSLMAS
VMRPSSMMRP SVVTDLSNNF SEAKIHDAHV QVFASDVLME GQLTKKGESG LQAWKNVSRI
FVLRGQELSY YTIDNKQRYG ALKGTWDIAG ASVERQDNSS FSLKLANGSI RTLGAPNVQT
LMDWMTAIAV AAEAHIVKPT SDLSLVDQSR TTHIILVRHG HYASSQTPSV DMHGPLTDLG
VQQARATGRF LHKYLSERMV LKRFPKFPVY HSGVRRAVET AERIGDAFPS GSLEFRENKL
FREAWPGNPL PNGNRQQLAR EKLDNMVSDC ARLKMAYRTM FRHLIPQDLE VNERQLSEED
LKHYANTFGI RSTQTRAKDR FRVVVCHANI IRWFVCKALG VDPDGTWGRM RYNHCGITAM
EVDSVGNVQL TYMNQTGHLE TTQLSEV
//