MTNC_SACEN
ID MTNC_SACEN Reviewed; 240 AA.
AC A4FFQ6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=SACE_3607;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAM02881.1; -; Genomic_DNA.
DR RefSeq; WP_009949019.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FFQ6; -.
DR SMR; A4FFQ6; -.
DR STRING; 405948.SACE_3607; -.
DR EnsemblBacteria; CAM02881; CAM02881; SACE_3607.
DR KEGG; sen:SACE_3607; -.
DR eggNOG; COG4229; Bacteria.
DR HOGENOM; CLU_023273_0_0_11; -.
DR OMA; QLKGHVY; -.
DR OrthoDB; 1204073at2; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000006728; 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; IPR023214; HAD_sf.
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..240
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000357394"
SQ SEQUENCE 240 AA; 25648 MW; 07AE1CDDEAF95FB3 CRC64;
MSASVAARWV VLDIEGTLTP TSQVHVVLYD YARPRLGPWI HDHPEDPVVR KAVEDVKSEA
GLPAEATAEQ VVAVLHGWMD ADRKAAPLKT LQGLIWQDGY ARGELTTDYF ADVVPALRAW
RQRGLVLAVF SSGSVAGQVA SFSHTTSGDL RGLFAQHFDT VNAGPKRERG SYEAIAAALG
AARPLQIVFL SDVPAELDAA AQAGWHTVGL ARPGEPYADA DFGSHPAVGA FDDIDIEVVS