ID   MTNB_ZYGRC              Reviewed;         243 AA.
AC   C5E0B9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE            Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE            EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03116};
GN   Name=MDE1 {ECO:0000255|HAMAP-Rule:MF_03116};
GN   OrderedLocusNames=ZYRO0G11440g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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_03116}.
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_03116};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03116};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03116};
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_03116}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03116}.
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DR   EMBL; CU928179; CAR29553.1; -; Genomic_DNA.
DR   RefSeq; XP_002498486.1; XM_002498441.1.
DR   AlphaFoldDB; C5E0B9; -.
DR   SMR; C5E0B9; -.
DR   STRING; 559307.C5E0B9; -.
DR   EnsemblFungi; CAR29553; CAR29553; ZYRO0G11440g.
DR   GeneID; 8206297; -.
DR   KEGG; zro:ZYRO0G11440g; -.
DR   HOGENOM; CLU_006033_4_0_1; -.
DR   InParanoid; C5E0B9; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000008536; Chromosome G.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_03116; Salvage_MtnB_euk; 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   InterPro; IPR027514; Salvage_MtnB_euk.
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; Cytoplasm; Lyase; Metal-binding;
KW   Methionine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..243
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000393857"
FT   ACT_SITE        131
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ   SEQUENCE   243 AA;  27280 MW;  6E40CF7CB7515381 CRC64;
     MPTDADYLID SQDPRHPANL ICTLCKQFFD FNWCTGTGGG ISIKHPQTGH LYVAPSGVQK
     EQMKPHDMFV VDGKSYEYLR IPPGLKPSAC TPLFNACYKY KSAGAIVHTH SLNAVTCSLI
     FGQEFRIRGV EQIKAIPSDR KDPSTGKVLN LNWDDTCVIP IIENRPHEDQ LEDPLMETFE
     KYPHACAVIV RRHGIFVWGP TIEKAKVINE ALDYLMELAV KMHQLGIPPD CSVGQESKYI
     SKH