ID   MTNC_KLEAE              Reviewed;          26 AA.
AC   P0C8L5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Enolase-phosphatase E1;
DE            EC=3.1.3.77;
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
DE   Flags: Fragment;
GN   Name=mtnC;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX   PubMed=8227039; DOI=10.1016/s0021-9258(19)74533-5;
RA   Myers R.W., Wray J.W., Fish S., Abeles R.H.;
RT   "Purification and characterization of an enzyme involved in oxidative
RT   carbon-carbon bond cleavage reactions in the methionine salvage pathway of
RT   Klebsiella pneumoniae.";
RL   J. Biol. Chem. 268:24785-24791(1993).
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   -!- 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:0000269|PubMed:8227039};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8227039};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8227039};
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.
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.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8227039}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC       family. {ECO:0000305}.
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DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Direct protein sequencing; Hydrolase; Magnesium;
KW   Metal-binding; Methionine biosynthesis.
FT   CHAIN           <1..>26
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000357372"
FT   NON_TER         1
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  2881 MW;  8690012789529533 CRC64;
     MIXAIVTDIE GTTSDTXFVX NVLFPY