MTNC_PSESM
ID MTNC_PSESM Reviewed; 227 AA.
AC Q884P1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=PSPTO_2047;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO55565.1; -; Genomic_DNA.
DR RefSeq; NP_791870.1; NC_004578.1.
DR RefSeq; WP_005766869.1; NC_004578.1.
DR AlphaFoldDB; Q884P1; -.
DR SMR; Q884P1; -.
DR STRING; 223283.PSPTO_2047; -.
DR EnsemblBacteria; AAO55565; AAO55565; PSPTO_2047.
DR GeneID; 1183692; -.
DR KEGG; pst:PSPTO_2047; -.
DR PATRIC; fig|223283.9.peg.2078; -.
DR eggNOG; COG4229; Bacteria.
DR HOGENOM; CLU_023273_0_0_6; -.
DR OMA; QLKGHVY; -.
DR OrthoDB; 1204073at2; -.
DR PhylomeDB; Q884P1; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000002515; 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 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..227
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000357393"
SQ SEQUENCE 227 AA; 24671 MW; 055CC48F3F40B52B CRC64;
MPIKAILTDI EGTTSAVSFV FDVLFPFARA HLPDFVRQHA EQPQVAAQLQ AVRTQSAEPD
ADVERVIAIL LEWIAEDRKA TPLKALQGMV WEQGYNAGQL KGHVYPDAVD ALQHWHQQGY
RLFVYSSGSI QAQQLIFGCS EAGDLSGLFS GYFDTTSGPK REAQSYQTIA NATGFAAEEI
LFLSDIVEEL DAAKAAGMLT CGLARDGGVL AGHRHVNSFT LIDPASF
