ID MTNW_BACP2 Reviewed; 406 AA. AC A8FCG8; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 03-MAY-2023, entry version 85. 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=BPUM_1252; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). RN [2] RP SEQUENCE REVISION TO N-TERMINUS. RC STRAIN=SAFR-032; RX PubMed=27351589; DOI=10.1371/journal.pone.0157331; RA Stepanov V.G., Tirumalai M.R., Montazari S., Checinska A., RA Venkateswaran K., Fox G.E.; RT "Bacillus pumilus SAFR-032 Genome Revisited: Sequence Update and Re- RT Annotation."; RL PLoS ONE 11:e0157331-e0157331(2016). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000813; ABV61935.2; -; Genomic_DNA. DR RefSeq; WP_041815463.1; NZ_VEIC01000008.1. DR AlphaFoldDB; A8FCG8; -. DR SMR; A8FCG8; -. DR STRING; 315750.BPUM_1252; -. DR EnsemblBacteria; ABV61935; ABV61935; BPUM_1252. DR KEGG; bpu:BPUM_1252; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_9; -. DR OrthoDB; 9770811at2; -. DR UniPathway; UPA00904; UER00876. DR Proteomes; UP000001355; 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; IPR020878; RuBisCo_large_chain_AS. 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; 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; SFLDG00301; RuBisCO-like_proteins; 1. DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1. DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1. DR TIGRFAMs; TIGR03332; salvage_mtnW; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding; KW Methionine biosynthesis. FT CHAIN 1..406 FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase" FT /id="PRO_0000357286" FT ACT_SITE 94 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 169..172 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 169 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 171 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 172 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 332 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 354..355 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT MOD_RES 169 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" SQ SEQUENCE 406 AA; 44486 MW; E9E183E7C681E4ED CRC64; MSELLATYVL THREDEQVNR KAEQIALGLT VGSWTDLPQL KKEQLQKHKG RVEKVTEKFA PAENGLYQSE VTIAYPEANF SADIPAVLST IFGKLSLDGK VKLVDIQFSD RFKKSLPGPV FGIDGIRKKT GVFDRPLLMS IFKGVIGRDM TDLKEQLRLQ ALGGVDFIKD DEILFESPLA PFEDRIKEGK KILKETYEET GHRTLYAVHL TGRTFELRDR ARKAAELGAD ALLFNVFAYG LDVMQSLAED PDIRLPIMAH PAVSGALTSS PEYGFSHSLL LGKLNRYAGA DLSLFPSPYG SVALPKKDAF GIYEACVKED SVQKTFPVPS AGIHPGMVPV LMKDFGLDHV INAGGGIHGH PRGAIGGGKA FRSIIDAVIH GESIQEKTAS CQDLKAALEL WGRVVE //