MTNBX_BACLD
ID MTNBX_BACLD Reviewed; 427 AA.
AC Q65KJ7; Q62VZ5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Bifunctional enzyme MtnB/MtnX;
DE Includes:
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase;
DE Short=MTRu-1-P dehydratase;
DE EC=4.2.1.109;
DE Includes:
DE RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase;
DE Short=HK-MTPenyl-1-P phosphatase;
DE EC=3.1.3.87;
GN Name=mtnB/mtnX; OrderedLocusNames=BLi01516, BL03541;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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:0000250}.
CC -!- FUNCTION: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-
CC phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-
CC methylthiopentene (DHK-MTPene). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O =
CC 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC Xref=Rhea:RHEA:14481, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:49252, ChEBI:CHEBI:59505; EC=3.1.3.87;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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.
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 4/6.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HAD-like
CC hydrolase superfamily. MtnX family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldolase class II
CC family. MtnB subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000002; AAU23063.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU40417.1; -; Genomic_DNA.
DR RefSeq; WP_003181077.1; NC_006322.1.
DR AlphaFoldDB; Q65KJ7; -.
DR SMR; Q65KJ7; -.
DR STRING; 279010.BL03541; -.
DR PRIDE; Q65KJ7; -.
DR EnsemblBacteria; AAU23063; AAU23063; BL03541.
DR GeneID; 66216416; -.
DR KEGG; bld:BLi01516; -.
DR KEGG; bli:BL03541; -.
DR eggNOG; COG0235; Bacteria.
DR eggNOG; COG4359; Bacteria.
DR HOGENOM; CLU_641990_0_0_9; -.
DR OrthoDB; 1755462at2; -.
DR BioCyc; BLIC279010:BLI_RS07520-MON; -.
DR UniPathway; UPA00904; UER00875.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01677; Salvage_MtnB; 1.
DR HAMAP; MF_01680; Salvage_MtnX; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR017718; HAD-SF_hydro_IB_MtnX.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_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 SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
DR TIGRFAMs; TIGR03333; salvage_mtnX; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Lyase; Metal-binding;
KW Methionine biosynthesis; Multifunctional enzyme; Reference proteome; Zinc.
FT CHAIN 1..427
FT /note="Bifunctional enzyme MtnB/MtnX"
FT /id="PRO_0000358313"
FT REGION 1..221
FT /note="HK-MTPenyl-1-P phosphatase"
FT REGION 222..427
FT /note="MTRu-1-P dehydratase"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 48068 MW; 825E98EB6E197057 CRC64;
MRKPLIICDF DGTITTNDNI ISIMKQFAPE EWTALKDGVL SKDISIRDGV GRMFNLLPAS
LKEDITAYVL KQAETRPGFK EFVSFLDEKG LPFYVVSGGM DFFVYPLLEG IVGKDRIYCN
EAAFTSRNIE IRWPYPCDGG CGNDCGCCKP SIIRRLKGRD DFVVMIGDSV TDVEAAKCSD
LCIARDYLLR ECEELGLKHA AFGDFRDVRR ILEETAEVKE WMSEQKRQEL AEVKKELAER
DWFPATSGNL SIKVSEDPLR FLITASGKDK RKETEEDFLL ADEEGRPAET GHALKPSAET
LLHTYVYQHT NAGCCLHVHT VDNNVISELY AKEKQVTFRG QEIIKALGLW EEHAEVTVPI
IENSAHIPDL AADFAGHLSG DSGAVLIRSH GITVWGKTAF EAKRMLEAYE FLFSWHLKLK
ALQAYHV
