MTNB_XANOP
ID MTNB_XANOP Reviewed; 225 AA.
AC B2SM82;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
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=mtnB1 {ECO:0000255|HAMAP-Rule:MF_01677}; OrderedLocusNames=PXO_00848;
GN and
GN Name=mtnB2 {ECO:0000255|HAMAP-Rule:MF_01677}; OrderedLocusNames=PXO_06079;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACD59082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACD59273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000967; ACD59082.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000967; ACD59273.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_027703723.1; NC_010717.2.
DR AlphaFoldDB; B2SM82; -.
DR SMR; B2SM82; -.
DR STRING; 360094.PXO_00848; -.
DR EnsemblBacteria; ACD59082; ACD59082; PXO_00848.
DR EnsemblBacteria; ACD59273; ACD59273; PXO_06079.
DR KEGG; xop:PXO_00848; -.
DR KEGG; xop:PXO_06079; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_4_1_6; -.
DR OrthoDB; 599627at2; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000001740; 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..225
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000357117"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
SQ SEQUENCE 225 AA; 25142 MW; A237F90361AF0F41 CRC64;
MNATTAPLPY SAARLHELAH VLIANIRELA HAGWTPATSS NFSHRLDEQH AAITVSGRDK
GRLVEEDIMV VDFDGLAVGR PLRPSAETLL HTQLYRRFPE ICCVLHTHSP VQTIASRLYA
GSDVIRLEGY ELLKAFEGNT THETAVEVPV FANTQDMQVL AAQVDALLDK QSMWGYLIEG
HGLYAWGRNM AEARRHLEAF EFLLQCELEL LKLRGTRQVV PVPHS
