ID A0A1C7EDR0_9BACL Unreviewed; 407 AA.
AC A0A1C7EDR0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000256|HAMAP-Rule:MF_01679};
DE Short=DK-MTP-1-P enolase {ECO:0000256|HAMAP-Rule:MF_01679};
DE EC=5.3.2.5 {ECO:0000256|HAMAP-Rule:MF_01679};
DE AltName: Full=RuBisCO-like protein {ECO:0000256|HAMAP-Rule:MF_01679};
DE Short=RLP {ECO:0000256|HAMAP-Rule:MF_01679};
GN Name=mtnW {ECO:0000256|HAMAP-Rule:MF_01679};
GN ORFNames=BCM40_00535 {ECO:0000313|EMBL:ANU21909.1};
OS Planococcus donghaensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=414778 {ECO:0000313|EMBL:ANU21909.1, ECO:0000313|Proteomes:UP000092495};
RN [1] {ECO:0000313|Proteomes:UP000092495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22276 {ECO:0000313|Proteomes:UP000092495};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01679};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01679}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01679}.
CC -!- MISCELLANEOUS: Has no RuBP-carboxylation activity. {ECO:0000256|HAMAP-
CC Rule:MF_01679}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01679}.
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DR EMBL; CP016543; ANU21909.1; -; Genomic_DNA.
DR RefSeq; WP_065525044.1; NZ_CP016543.2.
DR AlphaFoldDB; A0A1C7EDR0; -.
DR STRING; 414778.BCM40_00535; -.
DR KEGG; pdg:BCM40_00535; -.
DR OrthoDB; 9770811at2; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000092495; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01679};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01679};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01679};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01679};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_01679}.
FT DOMAIN 6..104
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 124..403
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 171..174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 356..357
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT MOD_RES 171
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
SQ SEQUENCE 407 AA; 43946 MW; 13721CBE53C5B35F CRC64;
MSTLTATYQL YGKSGSFEQK AEGIALGLTI GSWTNLPLLE QEQLKHHKGN VVSIKEYEEN
PHPLKPGLIK AEVAIAYPSA NFSADLPAIL TTVFGKLSLD GEVKLLDLEF SDDLLKHFPG
PRFGIEEIRH TLGVTDRPLL MSIFKGVIGR DLEYLSTQLR HQALGGVDLV KDDEILFDNP
LTPFEKRITT GKEVLQQVFE ETGHRTLYAV NLSGRTSELR GKAKKARELG ADALLFNVHA
YGLDVMQELV EDEDIALPLM AHPAFSGAFT SSSFYGLATS LALGKLTRYA GADFSLFPSP
YGSVALEKAS ALSLGEELTK ENSLKRSFPV PSAGIHPGLV PLLMADYGID SVINAGGGVH
GHPAGAVGGG QAFRQAIDAV LQGETLQNAS KQHEQLQTAL ELWGSKN
//
