ID MTNB_BACSU Reviewed; 209 AA.
AC O31668;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase;
DE Short=MTRu-1-P dehydratase;
DE EC=4.2.1.109;
GN Name=mtnB; Synonyms=ykrY; OrderedLocusNames=BSU13610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; 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 BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=18391471; DOI=10.1271/bbb.70651;
RA Ashida H., Saito Y., Kojima C., Yokota A.;
RT "Enzymatic characterization of 5-methylthioribulose-1-phosphate dehydratase
RT of the methionine salvage pathway in Bacillus subtilis.";
RL Biosci. Biotechnol. Biochem. 72:959-967(2008).
CC -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate
CC (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
CC {ECO:0000269|PubMed:14551435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.9 uM for S-methyl-5-thio-D-ribulose 1-phosphate (at 25 degrees
CC Celsius) {ECO:0000269|PubMed:18391471};
CC Vmax=42.7 umol/min/mg enzyme (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:18391471};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:18391471};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. It loses most of its
CC activity at 55 degrees Celsius. {ECO:0000269|PubMed:18391471};
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 2/6.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18391471}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13234.1; -; Genomic_DNA.
DR PIR; A69864; A69864.
DR RefSeq; NP_389244.1; NC_000964.3.
DR RefSeq; WP_003244782.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31668; -.
DR SMR; O31668; -.
DR STRING; 224308.BSU13610; -.
DR PaxDb; 224308-BSU13610; -.
DR EnsemblBacteria; CAB13234; CAB13234; BSU_13610.
DR GeneID; 939320; -.
DR KEGG; bsu:BSU13610; -.
DR PATRIC; fig|224308.179.peg.1478; -.
DR eggNOG; COG0235; Bacteria.
DR InParanoid; O31668; -.
DR OrthoDB; 9805559at2; -.
DR PhylomeDB; O31668; -.
DR BioCyc; BSUB:BSU13610-MONOMER; -.
DR BioCyc; MetaCyc:BSU13610-MONOMER; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR HAMAP; MF_01677; Salvage_MtnB; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR NCBIfam; TIGR03328; salvage_mtnB; 1.
DR PANTHER; PTHR10640; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR10640:SF7; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Lyase; Metal-binding; Methionine biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..209
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000162937"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 209 AA; 23489 MW; D4E8BE3544026FAB CRC64;
MAAKQERWRE LAEVKRELAE RDWFPATSGN LSIKVTDEPL TFLVTASGKD KRKETVEDFL
LVDQNGEPAE SGHSLKPSAE TLLHTHLYNK TNAGCCLHVH TVNNNVISEL YGDQKKITFK
GQEIIKALGL WEENAEVTVP IIENPAHIPT LAALFAEEIS EDSGAVLIRN HGITAWGKTA
FEAKRVLEAY EFLFSYHLKL KTLEHQLVK
//
