MTNX_BACCR
ID MTNX_BACCR Reviewed; 219 AA.
AC Q819E7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=BC_4037;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP10956.1; -; Genomic_DNA.
DR RefSeq; NP_833755.1; NC_004722.1.
DR RefSeq; WP_000027460.1; NC_004722.1.
DR AlphaFoldDB; Q819E7; -.
DR SMR; Q819E7; -.
DR STRING; 226900.BC_4037; -.
DR EnsemblBacteria; AAP10956; AAP10956; BC_4037.
DR KEGG; bce:BC4037; -.
DR PATRIC; fig|226900.8.peg.4168; -.
DR HOGENOM; CLU_058495_2_1_9; -.
DR OMA; VPFHEFD; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000001417; 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;
KW Reference proteome.
FT CHAIN 1..219
FT /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT phosphatase"
FT /id="PRO_0000357478"
SQ SEQUENCE 219 AA; 25042 MW; AB6117303762775E CRC64;
MSIQVFCDFD GTITNNDNIM SIMEKFAPPE AEEVKNKILS QELSIQEGVS QLFQLIPTNL
HDDIIQFLIE TAEIRSGFHE FIQFVKENNI SFYVISGGMD FFVYPLLQGI IPKEQIYCNE
TDFSAEFITV KWPHSCDDHC QIHCGLCKSS LIRKLSDTDD FHIVIGDSIT DLQAAKQADK
VFARDFLITK CEENHIAYTP FETFQDVQAE LKLLLEVKA