MTNX_BACP2
ID MTNX_BACP2 Reviewed; 231 AA.
AC A8FCG9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=BPUM_1253;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV61936.1; -; Genomic_DNA.
DR RefSeq; WP_012009736.1; NZ_VEIC01000008.1.
DR AlphaFoldDB; A8FCG9; -.
DR SMR; A8FCG9; -.
DR STRING; 315750.BPUM_1253; -.
DR PRIDE; A8FCG9; -.
DR EnsemblBacteria; ABV61936; ABV61936; BPUM_1253.
DR KEGG; bpu:BPUM_1253; -.
DR eggNOG; COG4359; Bacteria.
DR HOGENOM; CLU_058495_2_1_9; -.
DR OMA; VPFHEFD; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000001355; 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..231
FT /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT phosphatase"
FT /id="PRO_0000357482"
SQ SEQUENCE 231 AA; 26706 MW; 0B43B9613DAAAB90 CRC64;
MKKPIVCCDF DGTITKNDNI IRIMKHFAPS EWTKLKDDVL TKEITIQEGV GQMFQLLKSD
QKEAIQSFIL EDTEIREGFK QFVDHVKKAD IPFYVLSGGM DFFVYPILEG IVEREDIYCN
HASFHEEHIQ IEWPHACDSQ CQNGCGCCKP SIIRELTREN DFIIMIGDSV TDVEAAKHAD
LTFARDYLLN ECKELGLVHK EYETFIDLKA QFDQIKEVKE WQTKRTSAGR S