MTNX_GEOTN
ID MTNX_GEOTN Reviewed; 220 AA.
AC A4ILL6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=GTNG_0842;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(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; CP000557; ABO66220.1; -; Genomic_DNA.
DR RefSeq; WP_011887037.1; NC_009328.1.
DR AlphaFoldDB; A4ILL6; -.
DR SMR; A4ILL6; -.
DR STRING; 420246.GTNG_0842; -.
DR EnsemblBacteria; ABO66220; ABO66220; GTNG_0842.
DR KEGG; gtn:GTNG_0842; -.
DR eggNOG; COG4359; Bacteria.
DR HOGENOM; CLU_058495_2_1_9; -.
DR OMA; VPFHEFD; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000001578; 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..220
FT /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT phosphatase"
FT /id="PRO_0000357486"
SQ SEQUENCE 220 AA; 24789 MW; EAB6B39A7847BE30 CRC64;
MKKQLVLFCD FDGTITENDN IIAIMKQFAP PEWEALKDDI LAERLSVQEG VGKMFSLLPS
ALKDEIVDFL LSTARLREGF REFVAFTKEK GIPLYIVSGG IDFFVYPMLD GLIDKERIFC
NGSDFSSEMI RITWPHACDG KCQNGCGCCK PSLLRKLARP DGYHVVIGDS ITDLAVAKQA
DYVLARDFLL KKCQELDLPH APFTTFFDVV DHLQRLEVIA
