MTNX_BACCN
ID MTNX_BACCN Reviewed; 219 AA.
AC A7GS61;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01680};
DE Short=HK-MTPenyl-1-P phosphatase {ECO:0000255|HAMAP-Rule:MF_01680};
DE EC=3.1.3.87 {ECO:0000255|HAMAP-Rule:MF_01680};
GN Name=mtnX {ECO:0000255|HAMAP-Rule:MF_01680}; OrderedLocusNames=Bcer98_2736;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- FUNCTION: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-
CC phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-
CC methylthiopentene (DHK-MTPene). {ECO:0000255|HAMAP-Rule:MF_01680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O =
CC 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC Xref=Rhea:RHEA:14481, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:49252, ChEBI:CHEBI:59505; EC=3.1.3.87;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01680};
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_01680}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family.
CC {ECO:0000255|HAMAP-Rule:MF_01680}.
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DR EMBL; CP000764; ABS22969.1; -; Genomic_DNA.
DR RefSeq; WP_012095194.1; NC_009674.1.
DR AlphaFoldDB; A7GS61; -.
DR SMR; A7GS61; -.
DR STRING; 315749.Bcer98_2736; -.
DR EnsemblBacteria; ABS22969; ABS22969; Bcer98_2736.
DR GeneID; 56418279; -.
DR KEGG; bcy:Bcer98_2736; -.
DR eggNOG; COG4359; Bacteria.
DR HOGENOM; CLU_058495_2_1_9; -.
DR OMA; VPFHEFD; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; 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 Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01680; Salvage_MtnX; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR017718; HAD-SF_hydro_IB_MtnX.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
DR TIGRFAMs; TIGR03333; salvage_mtnX; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis.
FT CHAIN 1..219
FT /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT phosphatase"
FT /id="PRO_0000357477"
SQ SEQUENCE 219 AA; 25411 MW; A6AAD3C390C92369 CRC64;
MSIQIFCDFD GTITNSDNIT SIMEHFAPPK AEEIKKQILA QELSIQEGVE QLFHLLPTNL
HDDMIAFLKN NASIRSGFQE FVQFINKNDL SFYVILGGMD FFVHPLLDGL VPKEKIYCNE
TDFSKEYIEV KWPYPCDKHC NHHCGLCKST LIRRLSSQQD FRIVIGDSIT DLQAAKQADK
VFARDFLITK CKEYHIPYTP FHTFYDIQNE LQHLVEVKL