ID A0A1Y1W7I7_9FUNG Unreviewed; 240 AA.
AC A0A1Y1W7I7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=DL89DRAFT_267697 {ECO:0000313|EMBL:ORX69493.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX69493.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX69493.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX69493.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX69493.1}.
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DR EMBL; MCFD01000007; ORX69493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1W7I7; -.
DR STRING; 61395.A0A1Y1W7I7; -.
DR OrthoDB; 275419at2759; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000193922; 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; 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:UP000193922};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03116}.
FT DOMAIN 23..217
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 134
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
SQ SEQUENCE 240 AA; 26835 MW; DABC32B34C14FC21 CRC64;
MASQDDIHST DLVRSTDKNH PANLIPELCQ LFYTLGWVTG TGGGISIRDG EHVFIAPSGV
QKERIEPSQL FVLELATRKI LRSPSPPIKP SACTPLFYNS YTMRGAGACI HTHSQNAVLA
TMLYDKEFVI SHQEMIKGIR RGSSSESLRF FDTLRVPIIE NTAEEENLTN RMAKAIEQYP
ETNAVLVRRH GVYVWGESWQ KAKTMAECYD YLFELAVRMK QLGIDPAAVT QATQDAIDGE
//
