MTNW_GEOSW
ID MTNW_GEOSW Reviewed; 413 AA.
AC C5D7U9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=GWCH70_0850;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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; CP001638; ACS23730.1; -; Genomic_DNA.
DR RefSeq; WP_012749526.1; NC_012793.1.
DR AlphaFoldDB; C5D7U9; -.
DR SMR; C5D7U9; -.
DR STRING; 471223.GWCH70_0850; -.
DR EnsemblBacteria; ACS23730; ACS23730; GWCH70_0850.
DR KEGG; gwc:GWCH70_0850; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
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 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..413
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_1000215902"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 173..176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 173
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 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 359..360
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT MOD_RES 173
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
SQ SEQUENCE 413 AA; 45389 MW; 8AAFC73C5BA9708F CRC64;
MSQVIATYLI HDEKDLEKKA EGIALGLTVG SWTDLPLLEQ EQLRKHKGVV VSVQELEENE
RANRYFGKRL KRGIVRIAYP SLNFSADIPA LLTTVFGKLS LDGEVRLLDL TFSDEWKRKF
PGPRFGIDEI RKKLDVYERP LLMSIFKGMI GRDLTYLSEQ LKQQALGGVD LVKDDEILFE
NELTPFEKRI TAGKAVLNEV YEKTGKRTLY AVNLTGKTFE LKEKAKRAVE LGADVLLFNV
FAYGLDVLQG LREDDEITIP IMAHPAFSGA LTPSEFYGIK ASLLLGKLLR LVGADFVLFP
SPYGSVALDK EEALGIAAEL TNDKEPFKRS FPVPSAGIHP GLVPLLFRDF GIDSIVNAGG
GIHGHPDGAA GGGRAFRAAI DAALAGKSLH EAARENEALR KAIDLWGAVE VTS
