MTNW_BACVZ
ID MTNW_BACVZ Reviewed; 404 AA.
AC A7Z3X4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000255|HAMAP-Rule:MF_01679};
DE Short=DK-MTP-1-P enolase {ECO:0000255|HAMAP-Rule:MF_01679};
DE EC=5.3.2.5 {ECO:0000255|HAMAP-Rule:MF_01679};
DE AltName: Full=RuBisCO-like protein {ECO:0000255|HAMAP-Rule:MF_01679};
DE Short=RLP {ECO:0000255|HAMAP-Rule:MF_01679};
GN Name=mtnW {ECO:0000255|HAMAP-Rule:MF_01679}; OrderedLocusNames=RBAM_013370;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
CC -!- FUNCTION: Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-
CC phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-
CC phosphate (HK-MTPenyl-1-P). {ECO:0000255|HAMAP-Rule:MF_01679}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate = 2-hydroxy-5-
CC methylsulfanyl-3-oxopent-1-enyl phosphate; Xref=Rhea:RHEA:18769,
CC ChEBI:CHEBI:58828, ChEBI:CHEBI:59505; EC=5.3.2.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01679};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01679};
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 3/6. {ECO:0000255|HAMAP-Rule:MF_01679}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01679}.
CC -!- MISCELLANEOUS: Has no RuBP-carboxylation activity. {ECO:0000255|HAMAP-
CC Rule:MF_01679}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01679}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS73700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000560; ABS73700.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_023356860.1; NC_009725.2.
DR AlphaFoldDB; A7Z3X4; -.
DR SMR; A7Z3X4; -.
DR STRING; 326423.RBAM_013370; -.
DR EnsemblBacteria; ABS73700; ABS73700; RBAM_013370.
DR KEGG; bay:RBAM_013370; -.
DR HOGENOM; CLU_031450_3_1_9; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000001120; Chromosome.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
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 CDD; cd08209; RLP_DK-MTP-1-P-enolase; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01679; Salvage_MtnW; 1.
DR InterPro; IPR017717; Diketo-Methiopentyl-P_enolase.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR TIGRFAMs; TIGR03332; salvage_mtnW; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding;
KW Methionine biosynthesis.
FT CHAIN 1..404
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_0000357284"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 166..169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT MOD_RES 166
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
SQ SEQUENCE 404 AA; 44032 MW; EC790D087FDE898B CRC64;
MSEVLATYLL TDTTDSEKRA EQIAAGLTVG SWTDLPLVKQ EQLRKHKGRV VKVEEKEGTS
ENETQSVITI AYPEVNFSRD IPAVLTTVFG KLSLDGKIKL TDLEFSEGFK RSLPGPKFGI
YGIRKLLGEF ERPLLMSIFK GVIGRDLADI KEQLRQQALG GVDLIKDDEI FFENELAPFE
TRIIEGKQVL KETREETGHK TLYAVNLTGR TAELRDKARR AAELGADALL LNVFAYGLDV
MQSLAEDKEI PLPIMAHPAV SGAFTSSPVY GLSHALLLGK LNRYCGADFS LFPSPYGSVA
LPKESALAIH DECVKDDVFH PSFAVPSAGI HPGMVPLLMR DFGIDHIINA GGGIHGHPKG
GEGGGKAFRA IIDAVLEAQP IEEKAASCKD LQLALDKWGR VEAV
