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 15-FEB-2017, entry version 65. 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=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., RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C., RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., RA Venkateswaran K., Highlander S.K., 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- CC methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5- CC methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P). CC {ECO:0000255|HAMAP-Rule:MF_01679}. CC -!- CATALYTIC ACTIVITY: 5-(methylthio)-2,3-dioxopentyl phosphate = 2- CC hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate. CC {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- CC Rule:MF_01679}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose CC 1-phosphate: 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. CC {ECO:0000255|HAMAP-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; NC_009848.4. DR ProteinModelPortal; A8FCG8; -. DR STRING; 315750.BPUM_1252; -. DR PRIDE; A8FCG8; -. DR KEGG; bpu:BPUM_1252; -. DR PATRIC; 18966327; VBIBacPum16546_1260. DR eggNOG; ENOG4105DT1; Bacteria. DR eggNOG; COG1850; LUCA. DR HOGENOM; HOG000230832; -. DR KO; K08965; -. DR OrthoDB; POG091B0343; -. DR UniPathway; UPA00904; UER00876. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. 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 biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway. 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; IPR017443; RuBisCO_lsu_fd_N. DR Pfam; PF00016; RuBisCO_large; 2. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 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; Complete proteome; Isomerase; Magnesium; KW Metal-binding; Methionine biosynthesis; Reference proteome. FT CHAIN 1 406 2,3-diketo-5-methylthiopentyl-1-phosphate FT enolase. FT /FTId=PRO_0000357286. FT REGION 169 172 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT REGION 354 355 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT ACT_SITE 94 94 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT METAL 169 169 Magnesium; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_01679}. FT METAL 171 171 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT METAL 172 172 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT BINDING 143 143 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT BINDING 260 260 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01679}. FT BINDING 332 332 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01679}. FT MOD_RES 169 169 N6-carboxylysine. {ECO:0000255|HAMAP- FT 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 //