MTNB_BACAN
ID MTNB_BACAN Reviewed; 212 AA.
AC Q81MJ0; Q6HTZ0; Q6KN70;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_01677};
GN Name=mtnB {ECO:0000255|HAMAP-Rule:MF_01677};
GN OrderedLocusNames=BA_4257, GBAA_4257, BAS3948;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
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:0000255|HAMAP-Rule:MF_01677}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01677};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01677};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01677};
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. {ECO:0000255|HAMAP-Rule:MF_01677}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01677}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01677}.
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DR EMBL; AE016879; AAP27978.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33374.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56249.1; -; Genomic_DNA.
DR RefSeq; NP_846492.1; NC_003997.3.
DR RefSeq; WP_000811328.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030198.1; NC_005945.1.
DR AlphaFoldDB; Q81MJ0; -.
DR SMR; Q81MJ0; -.
DR STRING; 260799.BAS3948; -.
DR DNASU; 1088836; -.
DR EnsemblBacteria; AAP27978; AAP27978; BA_4257.
DR EnsemblBacteria; AAT33374; AAT33374; GBAA_4257.
DR GeneID; 45023928; -.
DR KEGG; ban:BA_4257; -.
DR KEGG; bar:GBAA_4257; -.
DR KEGG; bat:BAS3948; -.
DR PATRIC; fig|198094.11.peg.4227; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_4_1_9; -.
DR OMA; IRGHGLY; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; 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; 3.40.225.10; -; 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 PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lyase; Metal-binding; Methionine biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..212
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000357063"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
SQ SEQUENCE 212 AA; 23911 MW; 0782B4DA78BD7021 CRC64;
MKQLFRQWYD LSEIKKELTT RNWFPATSGN ISIKVSHEPL TFLITASGKD KTKTTPDDFL
LVDHLGVPVL ETELRPSAET ILHTHIYNNT NAGCVLHVHT TDNNVITNLY SDAVTLQNQE
IIKALDIWEE GATIHIPIIE NHAHIPTLGE NFRKHIQGDS GAVLIRNHGI TVWGRDSFDA
KKRLEAYEFL FQFHIKLLSI QGGVSNGANS YS
