ID   MTNB_ARTOC              Reviewed;         249 AA.
AC   C5FEJ4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 60.
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}; ORFNames=MCYG_01116;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEQ28228.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS995701; EEQ28228.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002851012.1; XM_002850966.1.
DR   AlphaFoldDB; C5FEJ4; -.
DR   SMR; C5FEJ4; -.
DR   STRING; 63405.XP_002851012.1; -.
DR   EnsemblFungi; EEQ28228; EEQ28228; MCYG_01116.
DR   GeneID; 9228473; -.
DR   eggNOG; KOG2631; Eukaryota.
DR   HOGENOM; CLU_006033_4_0_1; -.
DR   OrthoDB; 1062330at2759; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
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..249
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000393830"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ   SEQUENCE   249 AA;  27775 MW;  6E9C6209ADA4DD38 CRC64;
     MVDIKPEQTQ EGNNNDHLVQ SDDPEHPANL IPELCRKFYS LGWVTGTGGG TSIRRGEHIF
     IAPSGVQKEL IKPNEIFVLS YPTPKYPPSA RKYIRKPSAL NPSACTPLFL AAFDRGAGCC
     IHTHSQWAVM VTLLVEREKG KSGCFEISNI EQIKGIPRGK GKGMLGFFDT LKIPIIENTA
     FEEDLTESLE KAMEEYPDTY AVLVRRHGIY VWGDTPAKAK TQCESLDYLF QLAVQMHAHS
     LPWVVNESA