MTNB_SORMK
ID MTNB_SORMK Reviewed; 273 AA.
AC D1ZJC1; F7VLT3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=SMAC_04853;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000001; CCC06461.1; -; Genomic_DNA.
DR RefSeq; XP_003347546.1; XM_003347498.1.
DR AlphaFoldDB; D1ZJC1; -.
DR SMR; D1ZJC1; -.
DR STRING; 771870.D1ZJC1; -.
DR EnsemblFungi; CCC06461; CCC06461; SMAC_04853.
DR GeneID; 10804978; -.
DR KEGG; smp:SMAC_04853; -.
DR VEuPathDB; FungiDB:SMAC_04853; -.
DR eggNOG; KOG2631; Eukaryota.
DR HOGENOM; CLU_006033_4_0_1; -.
DR InParanoid; D1ZJC1; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 1062330at2759; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000001881; 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..273
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000393852"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ SEQUENCE 273 AA; 30307 MW; FEC39AE33F9D7C6F CRC64;
MCPTCPPSAA SASSENNNTD NNDHLVLSSD SSHPANLIPA LCAKFWTLGW VTGTGGGASI
RDNDLVYLAP SGVQKELMKP EDIYVLSLAA QATSPNPKQR VYLRSPANYK PSQCTPLFLA
AFTKRNAGCC IHTHSHWAVL VTLLLERERS SKEGDEEKGK VFEINNIEQI KGFGRGFGKS
GNLGYHDTLR IPVIENTAHE EDLTEFLEEA MDKYPDTYAV LVRRHGVYVW GENVHKAKTM
CESLDYLFQL AVEMKQLGLP WITDIEPTIP TRK
