ID A0A372LU02_9BACI Unreviewed; 218 AA.
AC A0A372LU02;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_01680};
DE Short=HK-MTPenyl-1-P phosphatase {ECO:0000256|HAMAP-Rule:MF_01680};
DE EC=3.1.3.87 {ECO:0000256|HAMAP-Rule:MF_01680};
GN Name=mtnX {ECO:0000256|HAMAP-Rule:MF_01680};
GN ORFNames=D0469_03590 {ECO:0000313|EMBL:RFU71034.1};
OS Peribacillus saganii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=2303992 {ECO:0000313|EMBL:RFU71034.1, ECO:0000313|Proteomes:UP000264541};
RN [1] {ECO:0000313|EMBL:RFU71034.1, ECO:0000313|Proteomes:UP000264541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V47-23a {ECO:0000313|EMBL:RFU71034.1,
RC ECO:0000313|Proteomes:UP000264541};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01680}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family.
CC {ECO:0000256|HAMAP-Rule:MF_01680}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU71034.1}.
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DR EMBL; QVTE01000008; RFU71034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372LU02; -.
DR OrthoDB; 9804940at2; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000264541; Unassembled WGS sequence.
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 CDD; cd07524; HAD_Pase; 1.
DR Gene3D; 3.90.1470.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR NCBIfam; TIGR03333; salvage_mtnX; 1.
DR PANTHER; PTHR28181:SF2; PHOSPHORIC MONOESTER HYDROLASE; 1.
DR PANTHER; PTHR28181; UPF0655 PROTEIN YCR015C; 1.
DR Pfam; PF12710; HAD; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01680};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01680, ECO:0000313|EMBL:RFU71034.1};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01680};
KW Reference proteome {ECO:0000313|Proteomes:UP000264541}.
SQ SEQUENCE 218 AA; 24961 MW; 642835CE8BB5BFDA CRC64;
MRPIIFCDFD GTVTNSDNII ALMKQFAAPE WEAIAEAVLS KRISIREGVG NMFSLLESGQ
KEKYIDFLLE HTKIREGFAE FIDFVKENEI RFYIISGGMD FFIEPILKPF DLKYIYCNNA
KFDEEFIRIE WPNSCDDKCS NDCGCCKPSI MRNLAGPDDF TIVIGDSITD LEAAKKADLV
LARDFLKRKC EQEGIAHLPF ETFHDCKAAL KNRLEVII
//
