ID A0A9P4Q1M3_9PEZI Unreviewed; 278 AA.
AC A0A9P4Q1M3;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 05-FEB-2025, entry version 6.
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=K431DRAFT_289175 {ECO:0000313|EMBL:KAF2716711.1};
OS Polychaeton citri CBS 116435.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Capnodiales; Capnodiaceae; Polychaeton.
OX NCBI_TaxID=1314669 {ECO:0000313|EMBL:KAF2716711.1, ECO:0000313|Proteomes:UP000799441};
RN [1] {ECO:0000313|EMBL:KAF2716711.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 116435 {ECO:0000313|EMBL:KAF2716711.1};
RA Haridas S., Albert R., Binder M., Bloem J., LaButti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
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=5-(methylsulfanyl)-D-ribulose 1-phosphate = 5-methylsulfanyl-
CC 2,3-dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58548, ChEBI:CHEBI:58828;
CC EC=4.2.1.109; 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:KAF2716711.1}.
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DR EMBL; MU003864; KAF2716711.1; -; Genomic_DNA.
DR OrthoDB; 191080at2759; -.
DR Proteomes; UP000799441; 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-UniRule.
DR FunFam; 3.40.225.10:FF:000003; Methylthioribulose-1-phosphate dehydratase; 1.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000799441};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03116}.
FT DOMAIN 49..267
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
SQ SEQUENCE 278 AA; 30380 MW; F4E0B1CD75AA7CB2 CRC64;
MTPPTGDQES AIAGASQSRQ QLHPNGNDAL SDSTADALVL SSDPDHPANH ICELCRKFYG
HGWVTGTGGG VSIKHGDKIY IAPSGQQKEL MQPTDMFVLD YGTGQYLRRP QGFKPSACTP
LFLASFTLRG AGCCIHTHSQ WAVLITLLCE QFPLSLSEDS SSDRSVFSIN KIEQIKGISR
GGAGSQEIAE GGRKLGNLGF FDTMKIPIIE NTAHEEDLKD SLEAAIKEWP ETCAVLVRRH
GVYVWGRDVA QAKTQCESLD YLFQLAVEMR RLGLPWIS
//
