MTNB_XYLFT
ID MTNB_XYLFT Reviewed; 218 AA.
AC Q87C38;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_01677};
GN Name=mtnB {ECO:0000255|HAMAP-Rule:MF_01677}; Synonyms=fucA2;
GN OrderedLocusNames=PD_1258;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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_01677}.
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_01677};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01677};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01677};
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_01677}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01677}.
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DR EMBL; AE009442; AAO29107.1; -; Genomic_DNA.
DR RefSeq; WP_004088323.1; NC_004556.1.
DR AlphaFoldDB; Q87C38; -.
DR SMR; Q87C38; -.
DR EnsemblBacteria; AAO29107; AAO29107; PD_1258.
DR GeneID; 58016790; -.
DR KEGG; xft:PD_1258; -.
DR HOGENOM; CLU_006033_4_1_6; -.
DR OMA; IRGHGLY; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 GO; GO:0005996; P:monosaccharide metabolic process; IEA:UniProt.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_01677; Salvage_MtnB; 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 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; Lyase; Metal-binding; Methionine biosynthesis;
KW Zinc.
FT CHAIN 1..218
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000357121"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
SQ SEQUENCE 218 AA; 24385 MW; AE4F564DCCB75154 CRC64;
MNATCTPSLP YDASRLRELA HLLIGTISEF AQAGWTPATS SNFSHRLDEH HVAITVSGRD
KRCLREEDIM AVDLDGNAVG HPHTPSAETL LHTQLYRRFP EIGCVLHTHS LTQTVASRVY
AGAGHISLKD YELLKAFAGH STHETTLDVP VFCNTQNMNI LAAQVDTLLD KQRMWGYLIN
GHGMYTWGNT LADARRHLEA LEFLLHCELD LLKLRGYL
