MTNC_KLEOX
ID MTNC_KLEOX Reviewed; 229 AA.
AC Q48389;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; Synonyms=masA;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M5a1;
RX PubMed=8227040; DOI=10.1016/s0021-9258(19)74534-7;
RA Balakrishnan R., Frohlich M., Rahaim P.T., Backman K., Yocum R.R.;
RT "Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the
RT methionine salvage pathway of Klebsiella oxytoca.";
RL J. Biol. Chem. 268:24792-24795(1993).
RN [2]
RP NOMENCLATURE.
RX PubMed=15102328; DOI=10.1186/1471-2180-4-9;
RA Sekowska A., Denervaud V., Ashida H., Michoud K., Haas D., Yokota A.,
RA Danchin A.;
RT "Bacterial variations on the methionine salvage pathway.";
RL BMC Microbiol. 4:9-9(2004).
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; U00148; AAC43183.1; -; Unassigned_DNA.
DR PIR; A49101; A49101.
DR RefSeq; WP_024358822.1; NZ_QPKC01000010.1.
DR AlphaFoldDB; Q48389; -.
DR BMRB; Q48389; -.
DR SMR; Q48389; -.
DR STRING; 571.MC52_16265; -.
DR eggNOG; COG4229; Bacteria.
DR BioCyc; MetaCyc:MON-1331; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
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.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Methionine biosynthesis.
FT CHAIN 1..229
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000357373"
FT REGION 206..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 25614 MW; DD3991CD71C5D2D1 CRC64;
MIRAIVTDIE GTTSDIRFVH NVLFPYARER LAGFVTAQQF VEPVKTILDN LREEIAQPAA
GAEELIATLF AFMDEDRKST ALKALQGIIW RDGYVHGDFT GHLYPDVLPA LEKWKSQGID
LYVYSSGSVA AQKLLFGYSD EGDITHLFNG YFDTLVGAKR EAQSYRNIAE QLGQPPAAIL
FLSDIHQELD AAEEAGFRTL QLVRGDRDPA SHHPQVQRFD DIHPEQIPA
