MTNW_BACC7
ID MTNW_BACC7 Reviewed; 414 AA.
AC B7HN14;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=BCAH187_A4167;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001177; ACJ78059.1; -; Genomic_DNA.
DR RefSeq; WP_000014185.1; NC_011658.1.
DR AlphaFoldDB; B7HN14; -.
DR SMR; B7HN14; -.
DR EnsemblBacteria; ACJ78059; ACJ78059; BCAH187_A4167.
DR KEGG; bcr:BCAH187_A4167; -.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000002214; 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..414
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_1000187379"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 174..177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 174
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 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 360..361
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT MOD_RES 174
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
SQ SEQUENCE 414 AA; 45483 MW; F5A85F73404FBDDB CRC64;
MSGIIATYLI HDDSHNLEKK AEQIALGLTI GSWTHLPHLL QEQLKQHKGN VIHVEELAEH
EHTNSYLRKK VKRGIIKIEY PLLNFSPDLP AILTTTFGKL SLDGEVKLID LTFSDELKKH
FPGPKFGIDG IRNLLQVHDR PLLMSIFKGM IGRNIGYLKT QLRDQAIGGV DIVKDDEILF
ENALTPLTKR IVSGKEVLQS VYETYGHKTL YAVNLTGRTF DLKENAKRAV QAGADILLFN
VFSYGLDVLQ SLAEDDEIPV PIMAHPAVSG AYSASKLYGV SSPLLLGKLL RYAGADFSLF
PSPYGSVALE KEEALAISKY LTEDDAFFKK SFSVPSAGIH PGFVPFIVRD FGKDVVINAG
GGIHGHPNGA QGGGKAFRAA IDATLQNKPL HEVDDINLHS ALQIWGNPSH EVKL
