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Database: UniProt
Entry: A0A3D9IFA9_9BACL
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ID   A0A3D9IFA9_9BACL        Unreviewed;       229 AA.
AC   A0A3D9IFA9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_01680};
DE            Short=HK-MTPenyl-1-P phosphatase {ECO:0000256|HAMAP-Rule:MF_01680};
DE            EC=3.1.3.87 {ECO:0000256|HAMAP-Rule:MF_01680};
GN   Name=mtnX {ECO:0000256|HAMAP-Rule:MF_01680};
GN   ORFNames=DFP95_106180 {ECO:0000313|EMBL:RED60390.1};
OS   Cohnella lupini.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1294267 {ECO:0000313|EMBL:RED60390.1, ECO:0000313|Proteomes:UP000256869};
RN   [1] {ECO:0000313|EMBL:RED60390.1, ECO:0000313|Proteomes:UP000256869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8236 {ECO:0000313|EMBL:RED60390.1,
RC   ECO:0000313|Proteomes:UP000256869};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-
CC       phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-
CC       methylthiopentene (DHK-MTPene). {ECO:0000256|HAMAP-Rule:MF_01680}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O =
CC         1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC         Xref=Rhea:RHEA:14481, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:49252, ChEBI:CHEBI:59505; EC=3.1.3.87;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01680};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC       step 4/6. {ECO:0000256|HAMAP-Rule:MF_01680}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family.
CC       {ECO:0000256|HAMAP-Rule:MF_01680}.
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:RED60390.1}.
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DR   EMBL; QRDY01000006; RED60390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9IFA9; -.
DR   OrthoDB; 9804940at2; -.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000256869; Unassembled WGS sequence.
DR   GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   CDD; cd07524; HAD_Pase; 1.
DR   Gene3D; 3.90.1470.20; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   HAMAP; MF_01680; Salvage_MtnX; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR017718; HAD-SF_hydro_IB_MtnX.
DR   InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   PANTHER; PTHR28181:SF2; PHOSPHORIC MONOESTER HYDROLASE; 1.
DR   PANTHER; PTHR28181; UPF0655 PROTEIN YCR015C; 1.
DR   Pfam; PF12710; HAD; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01680};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01680};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01680};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256869}.
SQ   SEQUENCE   229 AA;  25597 MW;  C336B1CB0FC1BE5C CRC64;
     MSNTTTRFPR PPVLFCDFDG TITLSDNIVA VMKHFNPPGW ENIVQQILNE TKSIRQGVGE
     MFSLLPSSMK EEVTSYILNS AGIRDGFAEL LEWCKKNDVP FYVTSGGIDF FVYPLLEPFG
     IPADHIYCNG SDFSGERIEI VWPHACDSEC DNGGCGMCKT AVIRRFPSDR FYRILIGDSV
     TDFAGAKLVD LVFSRSHLTV KCQELGLPHI PFETFHDIIK RLDQGGADS
//
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