ID L7UMT9_MYXSD Unreviewed; 230 AA.
AC L7UMT9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 OrderedLocusNames=MYSTI_06511 {ECO:0000313|EMBL:AGC47784.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC47784.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC47784.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
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};
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DR EMBL; CP004025; AGC47784.1; -; Genomic_DNA.
DR RefSeq; WP_015352038.1; NC_020126.1.
DR AlphaFoldDB; L7UMT9; -.
DR STRING; 1278073.MYSTI_06511; -.
DR KEGG; msd:MYSTI_06511; -.
DR PATRIC; fig|1278073.3.peg.6611; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_084200_0_0_7; -.
DR OMA; WQIVNTS; -.
DR OrthoDB; 280692at2; -.
DR Proteomes; UP000011131; Chromosome.
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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}.
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 230 AA; 25607 MW; DD6695460DD2181D CRC64;
MGAVYLIRHG QASFGAANYD QLSETGYVQA RVLGEALKAR QTKVDTVVMG TLARHQQTAE
TCLKALGTEI APTRIPGFNE FDHVELIVRH TPRYADHAAW MEDLATAPDP HRAIQDMFGQ
AVARWLAGQH DHEYAESWPA FQQRCIRALD SLIQDLGPSK TALVFTSGGP VTAICQHLLH
IPDEHAFRLN WTLANCGITK VVYSDRGHHL STLNEHAHFE GPHRGLVTYR
//