ID   MTNX_BACAH              Reviewed;         219 AA.
AC   A0RI43;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=BALH_3654;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK86886.1; -; Genomic_DNA.
DR   RefSeq; WP_000027477.1; NC_008600.1.
DR   AlphaFoldDB; A0RI43; -.
DR   SMR; A0RI43; -.
DR   EnsemblBacteria; ABK86886; ABK86886; BALH_3654.
DR   KEGG; btl:BALH_3654; -.
DR   HOGENOM; CLU_058495_2_1_9; -.
DR   OMA; VPFHEFD; -.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000000761; 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.
DR   TIGRFAMs; TIGR03333; salvage_mtnX; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis.
FT   CHAIN           1..219
FT                   /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT                   phosphatase"
FT                   /id="PRO_0000357474"
SQ   SEQUENCE   219 AA;  25290 MW;  D812BC6E0113738F CRC64;
     MSIQVFCDFD GTITNNDNIM SIMEKFAPPE AEEVKNRILS QELSIQEGVS QLFQLIPTNL
     HDEIIQFLIE TAEIRNGFHE FIQFVNENNI SFYVISGGMD FFVYPLLQGL IPKEQIYCNE
     TDFSNEYITV NWPHPCDRLC QNHCGLCKSS LIRKLSDTND FHIVIGDSIT DLQAAKQADK
     VFARDFLITK CEENHISYTP FETFHDVQTE LKHLLEVKL