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Database: UniProt
Entry: A0A0P6W4N0_9BACI
LinkDB: A0A0P6W4N0_9BACI
Original site: A0A0P6W4N0_9BACI 
ID   A0A0P6W4N0_9BACI        Unreviewed;       404 AA.
AC   A0A0P6W4N0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ECO:0000313|EMBL:KPL61335.1};
GN   ORFNames=AM506_01510 {ECO:0000313|EMBL:KPL61335.1};
OS   Rossellomorea vietnamensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL61335.1, ECO:0000313|Proteomes:UP000050398};
RN   [1] {ECO:0000313|EMBL:KPL61335.1, ECO:0000313|Proteomes:UP000050398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL61335.1,
RC   ECO:0000313|Proteomes:UP000050398};
RA   Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT   "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL   Submitted (AUG-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPL61335.1}.
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DR   EMBL; LIXZ01000001; KPL61335.1; -; Genomic_DNA.
DR   RefSeq; WP_060670101.1; NZ_LIXZ01000001.1.
DR   AlphaFoldDB; A0A0P6W4N0; -.
DR   PATRIC; fig|218284.4.peg.316; -.
DR   eggNOG; COG1850; Bacteria.
DR   OrthoDB; 9770811at2; -.
DR   UniPathway; UPA00904; UER00876.
DR   Proteomes; UP000050398; Unassembled WGS sequence.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000050398}.
FT   DOMAIN          2..94
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          118..398
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         165..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         165
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         167
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         351..352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   MOD_RES         165
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
SQ   SEQUENCE   404 AA;  43785 MW;  22A9BBB9E8C8B122 CRC64;
     MSEVIATYQL KGKSGSFGKK AEGIALGLTV GSWTDLPLLE QEQLRKYKGR VVSVEDWEDD
     DGSRAEVKIG YPGHNYSNDI PAILTTVFGK LSLDGEVKLL DLDFSEDLKK SYPGPRYGIE
     GIRELTGVYE RPLLMSIFKG VIGRDLTFLE NQLRAQALGG VNVVKDDEIL FDNSLTPFYE
     RVRLGKKVLD GVFEETGKRT LYAVNLTGKT SQLRDKARKA SEFGADALLF NVFSYGLDVL
     QELREDPEIS LPIMAHPAFA GAAAASPQYG VSYSLWLGKL LRMAGADFSL FPSPYGSVAL
     EKSNVLSISR ELTKDDAHLK KTLPVPSAGI HPALVPLLVK DFGTDCVINA GGGIHGHPDG
     AIGGGRAFVQ AIDAVLNGTS LREAAKTHEE LEKALSLWGG EVKV
//
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