ID   MTNC_STRM5              Reviewed;         231 AA.
AC   B4STR0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 96.
DE   RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_01681};
DE            EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_01681};
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_01681};
GN   Name=mtnC {ECO:0000255|HAMAP-Rule:MF_01681};
GN   OrderedLocusNames=Smal_1780;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-
CC       diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC       intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-
CC       MTPenyl-1-P), which is then dephosphorylated to form the acireductone
CC       1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
CC       {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
CC         dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC         Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01681};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01681};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01681};
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 3/6. {ECO:0000255|HAMAP-Rule:MF_01681}.
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_01681}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC       family. {ECO:0000255|HAMAP-Rule:MF_01681}.
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DR   EMBL; CP001111; ACF51484.1; -; Genomic_DNA.
DR   RefSeq; WP_012510902.1; NC_011071.1.
DR   AlphaFoldDB; B4STR0; -.
DR   SMR; B4STR0; -.
DR   STRING; 391008.Smal_1780; -.
DR   PaxDb; 391008-Smal_1780; -.
DR   KEGG; smt:Smal_1780; -.
DR   eggNOG; COG4229; Bacteria.
DR   HOGENOM; CLU_023273_0_0_6; -.
DR   OrthoDB; 9797416at2; -.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01629; HAD_EP; 1.
DR   Gene3D; 1.10.720.60; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   HAMAP; MF_01681; Salvage_MtnC; 1.
DR   InterPro; IPR023943; Enolase-ppase_E1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01691; enolase-ppase; 1.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   PANTHER; PTHR20371; ENOLASE-PHOSPHATASE E1; 1.
DR   PANTHER; PTHR20371:SF1; ENOLASE-PHOSPHATASE E1; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01133; C1.5.4:_Enolase-phosphatase_Li; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Methionine biosynthesis.
FT   CHAIN           1..231
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000357415"
SQ   SEQUENCE   231 AA;  25646 MW;  F21F8E325790548B CRC64;
     MQPRVILTDI EGTTSSISFV KNVLFPYARK ALPAFVAEHG QQPEVRRWLD AVATEIGGAC
     QDSLVAETLQ GWIDQDRKHT ALKALQGLIW DEGYRRGDYT AHFYPEVAPV LKGWHASGLP
     LYVYSSGSVP AQKLFFGFSD AGDLSPLVSG WFDTEIGGKR EADSYRRIVQ AIDVPAGEIL
     FLSDVVEELD AAREAGLQTR LIDRLDDYPL PRTGQAANGH ERVENFQQIQ L
//