ID E4ZVD0_LEPMJ Unreviewed; 241 AA.
AC E4ZVD0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_03116};
DE Short=MTRu-1-P dehydratase {ECO:0000256|HAMAP-Rule:MF_03116};
DE EC=4.2.1.109 {ECO:0000256|HAMAP-Rule:MF_03116};
GN Name=MDE1 {ECO:0000256|HAMAP-Rule:MF_03116};
GN ORFNames=LEMA_P027080.1 {ECO:0000313|EMBL:CBX95556.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_03116};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03116};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03116}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03116}.
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DR EMBL; FP929127; CBX95556.1; -; Genomic_DNA.
DR RefSeq; XP_003839035.1; XM_003838987.1.
DR AlphaFoldDB; E4ZVD0; -.
DR STRING; 985895.E4ZVD0; -.
DR EnsemblFungi; CBX95556; CBX95556; LEMA_P027080.1.
DR GeneID; 13280942; -.
DR eggNOG; KOG2631; Eukaryota.
DR HOGENOM; CLU_006033_4_0_1; -.
DR InParanoid; E4ZVD0; -.
DR OMA; HGLYTWG; -.
DR OrthoDB; 275419at2759; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000002668; Genome.
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; Class II aldolase/adducin N-terminal domain; 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 NCBIfam; TIGR03328; salvage_mtnB; 1.
DR PANTHER; PTHR10640; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR10640:SF7; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03116}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03116};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03116};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03116};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03116}; Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03116}.
FT DOMAIN 22..229
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
SQ SEQUENCE 241 AA; 27251 MW; 0A82300A37E796B9 CRC64;
MTTLEQEAES LVHSSDPNHP ANHICTLCAK FYTLGWVRFT KKGGSAGTGG GTSIRHEDKI
YIAPSGVQKE LMKPTDMFVM DFNTKEYLRK PQVLKPSACT PLFLAAFERG AGCCIHTHSQ
WAVLVTLLVE RDFGLEACFE IEEIEQIKGI PKFRGGRENL GYYDRLQIPI IENTAHEEDL
RESLEAAMEK YPNSYAILVR RHGIYVWGDN VHKAKTQCES IDYILQLAVE MKKLGLPWTK
S
//
