ID   MTNW_ALKCK              Reviewed;         374 AA.
AC   Q5WH45;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative 2,3-diketo-5-methylthiopentyl-1-phosphate enolase;
DE            Short=DK-MTP-1-P enolase;
DE            EC=5.3.2.5;
DE   AltName: Full=RuBisCO-like protein;
DE            Short=RLP;
GN   Name=mtnW; OrderedLocusNames=ABC1775;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) 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 3/6.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Has no RuBP-carboxylation activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although this resembles mtnW of B.subtilis, its genomic
CC       context is different, it is too short and it is missing a Mg-binding
CC       residue. Thus it may not be a functional ortholog. {ECO:0000305}.
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DR   EMBL; AP006627; BAD64310.1; -; Genomic_DNA.
DR   RefSeq; WP_011246618.1; NC_006582.1.
DR   AlphaFoldDB; Q5WH45; -.
DR   SMR; Q5WH45; -.
DR   STRING; 66692.ABC1775; -.
DR   EnsemblBacteria; BAD64310; BAD64310; ABC1775.
DR   KEGG; bcl:ABC1775; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_9; -.
DR   OMA; IHGHPDG; -.
DR   OrthoDB; 848380at2; -.
DR   UniPathway; UPA00904; UER00876.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   PANTHER; PTHR42704; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Reference proteome.
FT   CHAIN           1..374
FT                   /note="Putative 2,3-diketo-5-methylthiopentyl-1-phosphate
FT                   enolase"
FT                   /id="PRO_0000062695"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  41069 MW;  58B33A22D6254F2B CRC64;
     MAQINAVYYV SDSNEFIEEK AEKMATGLTA KPWQEMPEAE KQESFAYKGK VVSINEDPSY
     GEGSIVTISF PVAYEVPDFP SILTTTYGRL SYEPNVKLLD LQFSNDLVER FPGPLYGIEG
     IRDLVEVEGR PLAMSVAKGA IGRSIDSFHE QMLAHSYGGI DIIQDDERLF EHNWTPYEQR
     VPAGLAAIAE AAERTGRTPL YVVNLTGKTF ELKERAREAI GLGAPALMLN VYAYGIDVLQ
     GLREDPEIDV PIFAHSSLTG MMTRSKQHGI ASRLLLGKLL RMAGADAVLF PSPYGRIGIN
     PEEAQRVKDQ LTMTTQMKRA FPIPSAGIDF QTIATVRQDF GEDVIINLGG SVHRYKGGVE
     AGGKAFIEAL NSAN