MTNW_MICAN
ID MTNW_MICAN Reviewed; 386 AA.
AC B0JTU1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, 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=MAE_13070;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(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}.
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DR EMBL; AP009552; BAG01129.1; -; Genomic_DNA.
DR RefSeq; WP_012264739.1; NC_010296.1.
DR AlphaFoldDB; B0JTU1; -.
DR SMR; B0JTU1; -.
DR STRING; 449447.MAE_13070; -.
DR PaxDb; B0JTU1; -.
DR EnsemblBacteria; BAG01129; BAG01129; MAE_13070.
DR KEGG; mar:MAE_13070; -.
DR PATRIC; fig|449447.4.peg.1206; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_3; -.
DR OMA; AHFPFIA; -.
DR OrthoDB; 848380at2; -.
DR BioCyc; MAER449447:MAE_RS05785-MON; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000001510; 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; 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; 1.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Reference proteome.
FT CHAIN 1..386
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_0000357292"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 157..160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 157
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 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT MOD_RES 157
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
SQ SEQUENCE 386 AA; 41549 MW; 49D48A65109214E0 CRC64;
MTIIVDYRFP PAINAEKQAK TIAIGQTAGT WSERHSHRQE QLQQHLGEVV GIREEADGYK
VARVRFPQIN VENDIASLLT MIFGKYSMAG AGKVVGVYLP ETYGTKAKVG ITGIRQRLGV
YDRPLVMAIF KPALGLSAQD HADILREVAF AGLDVIKDDE IMADLPVAPT HERLDCCRLV
LEEVRQQTGR NVLYAVNVTG KADELQRKAR LLVKHGANAL LLNVLTYGFS VLEALASDPA
IDVPIFAHPA FAGAMCAGSD TGLAYSVVLG TMMAHAGADA VLYPAAYGSL PFDPQEEGKI
RDILRDRNVF PVPSAGIRPG IVPQVLGDYG RNVILNAGTG IMDHPSGPAS GVRAFFEALA
RIEAGDSFDP ANLPEGALKQ AILEWG
