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 12-AUG-2020, entry version 79. 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; Firmicutes; 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). 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=ABV61935.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; ABV61935.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_041815463.1; NZ_VEIC01000008.1. DR SMR; A8FCG8; -. DR STRING; 315750.BPUM_1252; -. DR PRIDE; A8FCG8; -. DR EnsemblBacteria; ABV61935; ABV61935; BPUM_1252. DR KEGG; bpu:BPUM_1252; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_9; -. DR KO; K08965; -. DR OrthoDB; 848380at2; -. DR BioCyc; BPUM315750:G1G9U-1303-MONOMER; -. 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; -; 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; 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; PTHR42704; 1. DR Pfam; PF00016; RuBisCO_large; 2. 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. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding; KW Methionine biosynthesis; Reference proteome. FT CHAIN 1..406 FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase" FT /id="PRO_0000357286" FT REGION 169..172 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT REGION 354..355 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT ACT_SITE 94 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT METAL 169 FT /note="Magnesium; via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT METAL 171 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT METAL 172 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 143 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 260 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679" FT BINDING 332 FT /note="Substrate; via amide nitrogen" 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 //