ID A0A1U9RC51_9GAMM Unreviewed; 228 AA.
AC A0A1U9RC51;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Enolase-phosphatase E1 {ECO:0000256|HAMAP-Rule:MF_01681};
DE EC=3.1.3.77 {ECO:0000256|HAMAP-Rule:MF_01681};
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000256|HAMAP-Rule:MF_01681};
GN Name=mtnC {ECO:0000256|HAMAP-Rule:MF_01681};
GN ORFNames=B2G49_14725 {ECO:0000313|EMBL:AQU83713.1};
OS Halomonas sp. 'Soap Lake #7'.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1962264 {ECO:0000313|EMBL:AQU83713.1, ECO:0000313|Proteomes:UP000189672};
RN [1] {ECO:0000313|EMBL:AQU83713.1, ECO:0000313|Proteomes:UP000189672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU83713.1,
RC ECO:0000313|Proteomes:UP000189672};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AQU83713.1, ECO:0000313|Proteomes:UP000189672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU83713.1,
RC ECO:0000313|Proteomes:UP000189672};
RA Mormile M.R.;
RT "Halomonas from Soap Lake, Washington USA.";
RL Submitted (MAR-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_01681};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01681};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01681}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01681}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC family. {ECO:0000256|HAMAP-Rule:MF_01681}.
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DR EMBL; CP019915; AQU83713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9RC51; -.
DR STRING; 1962264.B2G49_14725; -.
DR KEGG; haso:B2G49_14725; -.
DR OrthoDB; 9797416at2; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000189672; 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; 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 PRINTS; PR00413; HADHALOGNASE.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01681};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01681};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01681};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01681};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_01681}.
SQ SEQUENCE 228 AA; 25024 MW; A7006913DA33D914 CRC64;
MSNPTVRAIV TDIEGTTTDI NFVHKVLFPY AHAKLPDFLR ANAATPAVAE QIDAVRSEMG
DPKATLEAVI NQLLHWIETD QKVTPLKALQ GMVWANGYQR GDFTGHLYSD VAPALRHWKE
AGKALYVYSS GSVQAQKLLF GYSDEGDLTS LFSDYFDTHI GHKRDAAAYQ RIVTELDLPA
DAVLFLSDVI EELDAAKQAG MQTLQLVREG TQAGTVHACV TSFDEIAL
//
