MTNX_BACSU
ID MTNX_BACSU Reviewed; 235 AA.
AC O31667;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase;
DE Short=HK-MTPenyl-1-P phosphatase;
DE EC=3.1.3.87;
GN Name=mtnX; Synonyms=ykrX; OrderedLocusNames=BSU13600;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP REVIEW.
RX PubMed=12022921; DOI=10.1186/1471-2180-2-8;
RA Sekowska A., Danchin A.;
RT "The methionine salvage pathway in Bacillus subtilis.";
RL BMC Microbiol. 2:8-8(2002).
RN [3]
RP FUNCTION.
RX PubMed=14551435; DOI=10.1126/science.1086997;
RA Ashida H., Saito Y., Kojima C., Kobayashi K., Ogasawara N., Yokota A.;
RT "A functional link between RuBisCO-like protein of Bacillus and
RT photosynthetic RuBisCO.";
RL Science 302:286-290(2003).
RN [4]
RP NOMENCLATURE.
RX PubMed=15102328; DOI=10.1186/1471-2180-4-9;
RA Sekowska A., Denervaud V., Ashida H., Michoud K., Haas D., Yokota A.,
RA Danchin A.;
RT "Bacterial variations on the methionine salvage pathway.";
RL BMC Microbiol. 4:9-9(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of (2633731) from Bacillus subtilis at 2.00 a
RT resolution.";
RL Submitted (MAY-2008) to the PDB data bank.
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:0000269|PubMed:14551435}.
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 -!- 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.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13233.1; -; Genomic_DNA.
DR PIR; H69863; H69863.
DR RefSeq; NP_389243.1; NC_000964.3.
DR RefSeq; WP_003245748.1; NZ_JNCM01000035.1.
DR PDB; 2FEA; X-ray; 2.00 A; A/B=1-235.
DR PDBsum; 2FEA; -.
DR AlphaFoldDB; O31667; -.
DR SMR; O31667; -.
DR STRING; 224308.BSU13600; -.
DR PaxDb; O31667; -.
DR PRIDE; O31667; -.
DR EnsemblBacteria; CAB13233; CAB13233; BSU_13600.
DR GeneID; 939331; -.
DR KEGG; bsu:BSU13600; -.
DR PATRIC; fig|224308.179.peg.1477; -.
DR eggNOG; COG4359; Bacteria.
DR InParanoid; O31667; -.
DR OMA; VPFHEFD; -.
DR BioCyc; BSUB:BSU13600-MON; -.
DR BioCyc; MetaCyc:BSU13600-MON; -.
DR BRENDA; 3.1.3.87; 658.
DR UniPathway; UPA00904; UER00877.
DR EvolutionaryTrace; O31667; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..235
FT /note="2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
FT phosphatase"
FT /id="PRO_0000096631"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:2FEA"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2FEA"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:2FEA"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2FEA"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:2FEA"
SQ SEQUENCE 235 AA; 27002 MW; 69DEF79012653229 CRC64;
MTTRKPFIIC DFDGTITMND NIINIMKTFA PPEWMALKDG VLSKTLSIKE GVGRMFGLLP
SSLKEEITSF VLEDAKIREG FREFVAFINE HEIPFYVISG GMDFFVYPLL EGIVEKDRIY
CNHASFDNDY IHIDWPHSCK GTCSNQCGCC KPSVIHELSE PNQYIIMIGD SVTDVEAAKL
SDLCFARDYL LNECREQNLN HLPYQDFYEI RKEIENVKEV QEWLQNKNAG ESSLK
