MTNX_BACAN
ID MTNX_BACAN Reviewed; 219 AA.
AC Q81MJ1; Q6HTZ1; Q6KN71;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
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};
GN OrderedLocusNames=BA_4256, GBAA_4256, BAS3947;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
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; AE016879; AAP27977.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33373.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56248.1; -; Genomic_DNA.
DR RefSeq; NP_846491.1; NC_003997.3.
DR RefSeq; WP_000027476.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030197.1; NC_005945.1.
DR AlphaFoldDB; Q81MJ1; -.
DR SMR; Q81MJ1; -.
DR STRING; 260799.BAS3947; -.
DR DNASU; 1088838; -.
DR EnsemblBacteria; AAP27977; AAP27977; BA_4256.
DR EnsemblBacteria; AAT33373; AAT33373; GBAA_4256.
DR GeneID; 45023927; -.
DR KEGG; ban:BA_4256; -.
DR KEGG; bar:GBAA_4256; -.
DR KEGG; bat:BAS3947; -.
DR PATRIC; fig|198094.11.peg.4226; -.
DR eggNOG; COG4359; Bacteria.
DR HOGENOM; CLU_058495_2_1_9; -.
DR OMA; VPFHEFD; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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_0000357475"
SQ SEQUENCE 219 AA; 25290 MW; D812BC72F313738F CRC64;
MSIQVFCDFD GTITNNDNIM SIMEKFAPPE AEEVKNRILS QELSIQEGVS QLFQLIPTNL
HDEIIQFLIE TAEIRNGFHE FIQFVNENNI SFYVISGGMD FFVYPLLQGL IPKEQIYCNE
TDFSNEYITV NWPHPCDRLC QNHCGLCKSS LIRKLSDTND FHIVIGDSIT DLQAAKQADK
VFARDFLITK CEENHISYTP FETFHDVKTE LKHLLEVKL
