ID   MTNB_XANC5              Reviewed;         217 AA.
AC   Q3BUE6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}; OrderedLocusNames=XCV1886;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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   -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01677}.
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DR   EMBL; AM039952; CAJ23563.1; -; Genomic_DNA.
DR   RefSeq; WP_011347193.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BUE6; -.
DR   SMR; Q3BUE6; -.
DR   STRING; 456327.BJD11_12995; -.
DR   EnsemblBacteria; CAJ23563; CAJ23563; XCV1886.
DR   KEGG; xcv:XCV1886; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_4_1_6; -.
DR   OMA; IRGHGLY; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000007069; 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   GO; GO:0005996; P:monosaccharide metabolic process; IEA:UniProt.
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   Zinc.
FT   CHAIN           1..217
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000357114"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
SQ   SEQUENCE   217 AA;  24262 MW;  F118E6B7277CB701 CRC64;
     MNATTAPLPY STTRLHELAH LLIANIRELA HAGWTPATSS NFSHRLDEQH AAITVSGRDK
     GRLVEENIMV VDFDGLAVGR PLRPSAETLL HTQLYRRFPE IGCVLHTHSP VQTIASRLYA
     GSGVIRLEGY ELLKAFDGNT THETAVEVPV FANTQDMQVL AAQVDALLDK QSMWGYLIEG
     HGLYAWGRNM AEARRHLEAF EFLLHCELEL LKLRGTR