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Database: UniProt
Entry: MTNW_BACLD
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Original site: MTNW_BACLD 
ID   MTNW_BACLD              Reviewed;         405 AA.
AC   Q65KJ8; Q62VZ6;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 110.
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};
GN   OrderedLocusNames=BLi01515, BL03540;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU40416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017333; AAU40416.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000002; AAU23062.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q65KJ8; -.
DR   SMR; Q65KJ8; -.
DR   STRING; 279010.BL03540; -.
DR   KEGG; bld:BLi01515; -.
DR   KEGG; bli:BL03540; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_9; -.
DR   UniPathway; UPA00904; UER00876.
DR   Proteomes; UP000000606; 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; 2.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl; 1.
DR   SFLD; SFLDS00014; RuBisCO; 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; Isomerase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Reference proteome.
FT   CHAIN           1..405
FT                   /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT                   /id="PRO_0000062691"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         166..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         166
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         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   BINDING         351..352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT   MOD_RES         166
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
SQ   SEQUENCE   405 AA;  44034 MW;  A25EA2DBF2AF655D CRC64;
     MSELLATYIL ADPGCDAEKR AEQIAIGLTV GSWTDLPLLK QEQLKKHKGR VVNVEETESE
     LGEKQATVTI AYPEANFTND IPAVLTTVFG KLSLDGKIKL ADLEFSRSFK QSLPGPKFGV
     YGIRKKIGEF ERPLLMSIFK GVIGRDMEDL KEQLRQQALG GVDLIKDDEI LFETGSAPFE
     KRITEGKKVL EEAFEETGRK TLYAVNLTGR TMELKAKARK AAELGADVLL LNVFAYGLDV
     LQSFAEDDDI PLPIMAHPAV SGALTSSPHY GFSHSLLLGK LNRYAGADFS LFPSPYGSVA
     LPKRDALAIY DECTKEDVFK PTFAVPSAGI HPGMVPLLMK DFGIDHIINA GGGIHGHPNG
     AAGGGRAFRA VIDAVLEAEP VEEKAKRSPD LKLALEKWGR VEVSV
//
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