ID   MTNX_BACCQ              Reviewed;         219 AA.
AC   B9IWQ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=BCQ_3827;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14255.1; -; Genomic_DNA.
DR   RefSeq; WP_000027468.1; NC_011969.1.
DR   AlphaFoldDB; B9IWQ0; -.
DR   SMR; B9IWQ0; -.
DR   EnsemblBacteria; ACM14255; ACM14255; BCQ_3827.
DR   KEGG; bcq:BCQ_3827; -.
DR   HOGENOM; CLU_058495_2_1_9; -.
DR   OMA; VPFHEFD; -.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000000441; 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_1000187388"
SQ   SEQUENCE   219 AA;  25298 MW;  5A90B45AC9C73FE3 CRC64;
     MSIQVFCDFD GTITNNDNIM SIMEKFAPPE AEEVKNRILS QELSIQEGVS QLFQFIPTNL
     HDEIIQFLIE TAEIRNGFHE FIQFVNENNI SFYVISGGMD FFVYPLLQGL IPKEQIYCNE
     TDFSNEYITV NWPHPCDRLC QNHCGLCKSS LIRKLSDTND FHIVIGDSIT DLQAAKQADK
     VFARDFLITK CEENHISYTA FETFHDVQTE LKHLLEVKL