ID   MTNX_EXISA              Reviewed;         216 AA.
AC   C4KZ51;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01680};
DE            Short=HK-MTPenyl-1-P phosphatase {ECO:0000255|HAMAP-Rule:MF_01680};
DE            EC=3.1.3.87 {ECO:0000255|HAMAP-Rule:MF_01680};
GN   Name=mtnX {ECO:0000255|HAMAP-Rule:MF_01680}; OrderedLocusNames=EAT1b_1437;
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC   unclassified Exiguobacterium.
OX   NCBI_TaxID=360911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b;
RX   PubMed=21460088; DOI=10.1128/jb.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01680}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family.
CC       {ECO:0000255|HAMAP-Rule:MF_01680}.
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DR   EMBL; CP001615; ACQ70364.1; -; Genomic_DNA.
DR   RefSeq; WP_012727483.1; NC_012673.1.
DR   AlphaFoldDB; C4KZ51; -.
DR   SMR; C4KZ51; -.
DR   STRING; 360911.EAT1b_1437; -.
DR   EnsemblBacteria; ACQ70364; ACQ70364; EAT1b_1437.
DR   KEGG; eat:EAT1b_1437; -.
DR   eggNOG; COG4359; Bacteria.
DR   HOGENOM; CLU_058495_2_1_9; -.
DR   OMA; VPFHEFD; -.
DR   OrthoDB; 1755462at2; -.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000000716; Chromosome.
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   Gene3D; 3.40.50.1000; -; 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   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..216
FT                   /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT                   phosphatase"
FT                   /id="PRO_1000215903"
SQ   SEQUENCE   216 AA;  24319 MW;  8DC8AEC19C20626B CRC64;
     MSTHVICDFD GTITEEDNII ALMRRFAPPE WVELKDSVLN QTLSIREGVG QMFSLLPSNQ
     QERYREFLQS TITLRAGFVE FLQETQSHGF RFDVVSGGMD FFVHPILEGH VAPEHIFCNH
     VDFSGETARV TWPHACDVHC LNDCGCCKPT IARQIVSPTD TLIVIGDSVT DFEIAKRADV
     VYARGQLISL CEAEGIRHVP FETFYDISAY MKGVNV