ID   MTNC_SHEPA              Reviewed;         226 AA.
AC   A8HAA3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
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}; OrderedLocusNames=Spea_4180;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000851; ABV89490.1; -; Genomic_DNA.
DR   RefSeq; WP_012157368.1; NC_009901.1.
DR   AlphaFoldDB; A8HAA3; -.
DR   SMR; A8HAA3; -.
DR   STRING; 398579.Spea_4180; -.
DR   EnsemblBacteria; ABV89490; ABV89490; Spea_4180.
DR   KEGG; spl:Spea_4180; -.
DR   eggNOG; COG4229; Bacteria.
DR   HOGENOM; CLU_023273_0_0_6; -.
DR   OMA; QLKGHVY; -.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000002608; Chromosome.
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   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; cd01629; HAD_EP; 1.
DR   Gene3D; 3.40.50.1000; -; 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   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000357405"
SQ   SEQUENCE   226 AA;  25197 MW;  3AADE00FFF9392D8 CRC64;
     MGIRAIVVDT AGTTTDLNFI EDVLFPYSAK ALPAFLEENQ NNVLVDNCIC DVQDIALEPD
     ASLARVTEIL LQWIEEDRKA TPLKTIQGLI WKQGYANGEF TGHIFPDFIE ALDGYKQQGL
     RVYSFSSGSV EAQKLLFSHS DAGDLNDKFN GHFDTRTGNK RFKQAYSNIV NTISLSPKQI
     LFVSDVLEEL KAANEAGLHV VQMVRDDSQR TGDFKTIASF DELKID