MTNW_BACAC
ID MTNW_BACAC Reviewed; 414 AA.
AC C3LIA6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-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}; OrderedLocusNames=BAMEG_4296;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP14181.1; -; Genomic_DNA.
DR RefSeq; WP_000014200.1; NC_012581.1.
DR AlphaFoldDB; C3LIA6; -.
DR SMR; C3LIA6; -.
DR GeneID; 45023926; -.
DR KEGG; bah:BAMEG_4296; -.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OMA; IHGHPDG; -.
DR UniPathway; UPA00904; UER00876.
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_1000187374"
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; 45525 MW; FB9BC6FC7CB27F51 CRC64;
MSGIIATYLI HDDSHNLEKK AEQIALGLTI GSWTHLPHLL QEQLKQHKGN VLHVEELAEH
EHTNSYLRKK VKRGIIKIEY PLLNFSPDLP AILTTTFGKL SLDGEVKLID LTFSDELKKH
FPGPKFGIDG IRNLLQVHDR PLLMSIFKGM IGRNIGYLKT QLRDQAIGGV DIVKDDEILF
ENALTPLTNR IVSGKEVLQS VYETYGHKTL YAVNVTGRTF DLKENAKRAV QAGADILLFN
VFAYGLDVLQ SLAEDDEIPV PIMAHPAVSG AYSASKLYGI SSPLLLGKLL RYAGADFSLF
PSPYGSVALE KEEALAISKY LTEDDVFFKK SFSVPSAGIH PGFVPFIIRD FGKDVVINAG
GGIHGHPNGA QGGGKAFRTA IDATLQNKPL HEVDDINLHS ALQIWGNPSH EVKL
