ID M5DL69_9GAMM Unreviewed; 230 AA.
AC M5DL69;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=TOL_0046 {ECO:0000313|EMBL:CCU70495.1};
OS Thalassolituus oleivorans MIL-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Thalassolituus.
OX NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU70495.1, ECO:0000313|Proteomes:UP000011866};
RN [1] {ECO:0000313|EMBL:CCU70495.1, ECO:0000313|Proteomes:UP000011866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIL-1 {ECO:0000313|EMBL:CCU70495.1,
RC ECO:0000313|Proteomes:UP000011866};
RX PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA Yakimov M.M., Teeling H., Golyshina O.V.;
RT "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL Genome Announc. 1:1-3(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; HF680312; CCU70495.1; -; Genomic_DNA.
DR RefSeq; WP_015485240.1; NC_020888.1.
DR AlphaFoldDB; M5DL69; -.
DR STRING; 187493.CN03_00800; -.
DR KEGG; tol:TOL_0046; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_084200_0_0_6; -.
DR Proteomes; UP000011866; 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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011866}.
SQ SEQUENCE 230 AA; 25776 MW; EEB16A7E89B0C475 CRC64;
MASIYLVRHG QAGFDKLNYD QLSELGFAQG ELVGKALAQR GIEAPMVVHG AMQRHRETMQ
SAQRHWHSFG PIVEMFGFNE FDSDDVIACA FPHFKHKAAL GAWLLTQKNR RKAFQELFAK
AVERWTSGEH DDDYIESWNN FTGRCTRALE DLITNAAGKN VVVFTSGGPV TAIAQHCLGL
SHDKAFELNW TLLNAGISQL LYNREGKVSL ASCNEHHHLA SAGKQYLTYR
//