MTNC_GLUOX
ID MTNC_GLUOX Reviewed; 227 AA.
AC Q5FRJ1; Q9RM33;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=GOX1244;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9937 / LMG 1404 / NCIMB 8084;
RX PubMed=10518757; DOI=10.1111/j.1574-6968.1999.tb08769.x;
RA Gupta A., Felder M., Verma V.V., Cullum J., Qazi G.N.;
RT "A mutant of gluconobacter oxydans deficient in gluconic acid
RT dehydrogenase.";
RL FEMS Microbiol. Lett. 179:501-506(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; AJ238888; CAB55632.1; -; Genomic_DNA.
DR EMBL; CP000009; AAW61005.1; -; Genomic_DNA.
DR RefSeq; WP_011252797.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FRJ1; -.
DR SMR; Q5FRJ1; -.
DR STRING; 290633.GOX1244; -.
DR EnsemblBacteria; AAW61005; AAW61005; GOX1244.
DR KEGG; gox:GOX1244; -.
DR eggNOG; COG4229; Bacteria.
DR HOGENOM; CLU_023273_0_0_5; -.
DR OMA; QLKGHVY; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000006375; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Reference proteome.
FT CHAIN 1..227
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000357368"
FT CONFLICT 42
FT /note="I -> T (in Ref. 1; CAB55632)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="G -> A (in Ref. 1; CAB55632)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> Q (in Ref. 1; CAB55632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 24321 MW; 5B61077957475E9A CRC64;
MIRLVLLDIE GTTLPISFVR DVMFPYAAKA LPALMQDHTN PIVVGARADI VMEHPGQDPL
KVCQDWMKAD VKAAPLKTLQ GLTWRQGFED GTLQADLYPD VPPALKAWSK GGLRLAVYSS
GSIPSQKLLY GHTAQGDLTP LFEDFFDLST GGKKDAASYE KITAAVGLPA DEILFLSDIG
AELDAAQRAG LSVCQLVREQ DGTVPHPGVP QAPDLNAVST QFGLPVA
