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Database: UniProt
Entry: MTNW_GEOKA
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ID   MTNW_GEOKA              Reviewed;         413 AA.
AC   Q5L1E2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=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=GK0953;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP   MAGNESIUM IONS, FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF LYS-98; LYS-147
RP   AND LYS-173, AND CARBOXYLATION AT LYS-173.
RX   PubMed=17352497; DOI=10.1021/bi7000483;
RA   Imker H.J., Fedorov A.A., Fedorov E.V., Almo S.C., Gerlt J.A.;
RT   "Mechanistic diversity in the RuBisCO superfamily: the 'enolase' in the
RT   methionine salvage pathway in Geobacillus kaustophilus.";
RL   Biochemistry 46:4077-4089(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:0000269|PubMed:17352497}.
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;
CC         Evidence={ECO:0000269|PubMed:17352497};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17352497};
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:0000269|PubMed:17352497}.
CC   -!- MISCELLANEOUS: Has no RuBP-carboxylation activity.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BA000043; BAD75238.1; -; Genomic_DNA.
DR   RefSeq; WP_011230454.1; NC_006510.1.
DR   PDB; 2OEJ; X-ray; 2.55 A; A/B=1-413.
DR   PDB; 2OEK; X-ray; 1.80 A; A/B=1-413.
DR   PDB; 2OEL; X-ray; 1.80 A; A/B=1-413.
DR   PDB; 2OEM; X-ray; 1.70 A; A/B=1-413.
DR   PDBsum; 2OEJ; -.
DR   PDBsum; 2OEK; -.
DR   PDBsum; 2OEL; -.
DR   PDBsum; 2OEM; -.
DR   AlphaFoldDB; Q5L1E2; -.
DR   SMR; Q5L1E2; -.
DR   STRING; 235909.GK0953; -.
DR   DrugBank; DB06881; (1Z)-2-HYDROXY-3-OXOHEX-1-EN-1-YL DIHYDROGEN PHOSPHATE.
DR   KEGG; gka:GK0953; -.
DR   PATRIC; fig|235909.7.peg.1041; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_9; -.
DR   BRENDA; 5.3.2.5; 8138.
DR   UniPathway; UPA00904; UER00876.
DR   EvolutionaryTrace; Q5L1E2; -.
DR   Proteomes; UP000001172; 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; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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   NCBIfam; TIGR03332; salvage_mtnW; 1.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 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; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Reference proteome.
FT   CHAIN           1..413
FT                   /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT                   /id="PRO_0000062694"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT   BINDING         147
FT                   /ligand="substrate"
FT   BINDING         173..176
FT                   /ligand="substrate"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         264
FT                   /ligand="substrate"
FT   BINDING         337
FT                   /ligand="substrate"
FT   BINDING         359..360
FT                   /ligand="substrate"
FT   MOD_RES         173
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000269|PubMed:17352497"
FT   MUTAGEN         98
FT                   /note="K->A: Loss of enolase activity."
FT                   /evidence="ECO:0000269|PubMed:17352497"
FT   MUTAGEN         147
FT                   /note="K->A: Same activity as the wild-type."
FT                   /evidence="ECO:0000269|PubMed:17352497"
FT   MUTAGEN         173
FT                   /note="K->A: Same activity as the wild-type."
FT                   /evidence="ECO:0000269|PubMed:17352497"
FT   STRAND          3..14
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           60..66
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          71..80
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           88..96
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          102..111
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           126..134
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           154..166
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           186..204
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          209..213
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           221..230
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           245..253
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          275..279
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           287..292
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           310..321
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          331..337
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           340..342
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           343..350
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   STRAND          352..359
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           360..363
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           368..385
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           389..393
FT                   /evidence="ECO:0007829|PDB:2OEM"
FT   HELIX           397..406
FT                   /evidence="ECO:0007829|PDB:2OEM"
SQ   SEQUENCE   413 AA;  44906 MW;  560DBEA2E17E0310 CRC64;
     MSAVMATYLL HDETDIRKKA EGIALGLTIG TWTDLPALEQ EQLRKHKGEV VAIEELGESE
     RVNAYFGKRL KRAIVKIAYP TVNFSADLPA LLVTTFGKLS LDGEVRLLDL EFPDEWKRQF
     PGPRFGIDGI RDRVGVHNRP LLMSIFKGMI GRDLAYLTSE LKKQALGGVD LVKDDEILFD
     SELLPFEKRI TEGKAALQEV YEQTGKRTLY AVNLTGKTFA LKDKAKRAAE LGADVLLFNV
     FAYGLDVLQA LREDEEIAVP IMAHPAFSGA VTPSEFYGVA PSLWLGKLLR LAGADFVLFP
     SPYGSVALER EQALGIARAL TDDQEPFARA FPVPSAGIHP GLVPLIIRDF GLDTIVNAGG
     GIHGHPDGAI GGGRAFRAAI DAVLAGRPLR AAAAENEALQ KAIDRWGVVE VEA
//
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