MTNB_LEPBL
ID MTNB_LEPBL Reviewed; 250 AA.
AC Q04WK2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; OrderedLocusNames=LBL_4232;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000349; ABJ80543.1; -; Genomic_DNA.
DR RefSeq; WP_011671396.1; NC_008509.1.
DR AlphaFoldDB; Q04WK2; -.
DR SMR; Q04WK2; -.
DR KEGG; lbl:LBL_4232; -.
DR HOGENOM; CLU_006033_4_1_12; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 599627at2; -.
DR UniPathway; UPA00904; UER00875.
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 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..250
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000357089"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
SQ SEQUENCE 250 AA; 28079 MW; 965FC8D5C34364C5 CRC64;
MSVKKQLEKL SILGATYHKN GWMPGTAGNL SVRILGESGF WVSGSGLDKN TLNKRNFLYV
DLKSGRLSPS KNTKVEKGLK PSAETSIHRA VYCALDDIGC GLHVHTLESN LIRTNTSQHR
PVALLELPAI EILKVYGIWK ESPKVYVPVI YNFPNVQDIS DCLESYLKEY KPVVPFCIIE
KHGITVWGKD TVQANRNLEA TDFILKYMIS SRNLSNPEGK KNFPTENNTS ESDRQKVYVA
EFPVYPATFL