ID   MTNB_GEOTN              Reviewed;         211 AA.
AC   A4ILL7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=GTNG_0843;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO66221.1; -; Genomic_DNA.
DR   RefSeq; WP_008878835.1; NC_009328.1.
DR   AlphaFoldDB; A4ILL7; -.
DR   SMR; A4ILL7; -.
DR   STRING; 420246.GTNG_0843; -.
DR   EnsemblBacteria; ABO66221; ABO66221; GTNG_0843.
DR   KEGG; gtn:GTNG_0843; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_4_1_9; -.
DR   OMA; IRGHGLY; -.
DR   OrthoDB; 599627at2; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000001578; 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   Zinc.
FT   CHAIN           1..211
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000357080"
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   211 AA;  23755 MW;  FA95B238C9B45C04 CRC64;
     MSIMLKKWNE LAEVKAELAA RDWFFATSGN LSLKVTDAPL TFLVTASGKD KRKQTSEDFL
     LIDADGKPVE DTHLKPSAET LLHVEVYRRT NAGCVLHVHT VDNNIISDVY AQNREAVFSG
     QEIIKAFGIW EENAEVRIPI IDNYADIPTL ANEFAKHIDG DTGAVLIQNH GITVWGRDAF
     EAKKHLEAWE FLFSWQVKRL LLQRAAVPLV D