MTNW_GEOKA
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 03-AUG-2022, entry version 107.
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; Firmicutes; 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 EnsemblBacteria; BAD75238; BAD75238; GK0953.
DR KEGG; gka:GK0953; -.
DR PATRIC; fig|235909.7.peg.1041; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OMA; IHGHPDG; -.
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; -; 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 SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR TIGRFAMs; TIGR03332; salvage_mtnW; 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
