ID   MTNC_SYNE7              Reviewed;         238 AA.
AC   Q31LP5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 116.
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=Synpcc7942_1994;
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; 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; CP000100; ABB58024.1; -; Genomic_DNA.
DR   RefSeq; WP_011244412.1; NC_007604.1.
DR   AlphaFoldDB; Q31LP5; -.
DR   SMR; Q31LP5; -.
DR   STRING; 1140.Synpcc7942_1994; -.
DR   PaxDb; 1140-Synpcc7942_1994; -.
DR   GeneID; 72430867; -.
DR   KEGG; syf:Synpcc7942_1994; -.
DR   eggNOG; COG4229; Bacteria.
DR   HOGENOM; CLU_023273_0_0_3; -.
DR   OrthoDB; 9797416at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1994-MONOMER; -.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000889800; 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   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; Reference proteome.
FT   CHAIN           1..238
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000357418"
SQ   SEQUENCE   238 AA;  25681 MW;  7510F066FDDCEA19 CRC64;
     MPLPVSITTL LLDIEGTTTP VDFVFKVLFP YARDRVADFL ATQGADPEVQ ADLDLLRQEY
     AQEAAAELPD WAGEDAIAAV PYIQWLIDSD RKSTGLKSLQ GKIWEQGYVS GEIKGQLFAD
     VLPAFQRWQA AGLAIAIFSS GSVQAQQLLF GYSEAGDLSP HLSGYFDTRT GPKREAASYG
     AIAAQLGKAP AQVLFVSDIP AELEAAATAG FQTRLSLRPG NATVEIGDWT TIHSFDEL
//