MTNW_MICAE
ID MTNW_MICAE Reviewed; 386 AA.
AC A8YER2; Q0P7L2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase;
DE Short=DK-MTP-1-P enolase;
DE EC=5.3.2.5;
DE AltName: Full=RuBisCO-like protein;
DE Short=RLP;
GN Name=mtnW; Synonyms=rbcLIV; ORFNames=IPF_2991;
OS Microcystis aeruginosa.
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=1126;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=PCC 7806;
RX PubMed=16737967; DOI=10.1074/jbc.m602973200;
RA Carre-Mlouka A., Mejean A., Quillardet P., Ashida H., Saito Y., Yokota A.,
RA Callebaut I., Sekowska A., Dittmann E., Bouchier C., de Marsac N.T.;
RT "A new Rubisco-like protein coexists with a photosynthetic Rubisco in the
RT planktonic cyanobacteria Microcystis.";
RL J. Biol. Chem. 281:24462-24471(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7806;
RA Frangeul L.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:16737967}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for 2,3-diketo-5-methylthiopentyl-1-phosphate (at pH 8 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:16737967};
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.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16737967}.
CC -!- MISCELLANEOUS: Has no RuBP-carboxylation activity.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000305}.
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DR EMBL; AM157794; CAJ43366.1; -; Genomic_DNA.
DR EMBL; AM778930; CAO89633.1; -; Genomic_DNA.
DR RefSeq; WP_002740716.1; NZ_CP046058.1.
DR AlphaFoldDB; A8YER2; -.
DR SMR; A8YER2; -.
DR UniPathway; UPA00904; UER00876.
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 SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding;
KW Methionine biosynthesis.
FT CHAIN 1..386
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_0000357291"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 157
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 41619 MW; 23BD981DD3DE3A0A CRC64;
MTIIVDYRFP PAINAEKQAK TIAIGQTAGT WSERHSHRQK QLQQHLAEVV GIREEADGYK
VARVRFPQIN VENDIASLLT MIFGKYSMAG AGKVVGVYLP ESYGTKAKLG ITGIRQRLGV
YDRPLVMAIF KPALGLSAQD HADILREVAF AGLDVIKDDE IMADLPVAPT HERLDCCRRV
LEEVRQQTGR NVLYAVNVTG KADELQRKAR LLVKHGANAL LLNVLTYGFS VLEALASDPA
IDVPIFAHPA FAGAMCAGSD TGLAYSVVLG TMMAHAGADA VLYPAAYGSL PFDPQEEGKI
RDILRDRNVF PVPSAGIRPG IVPQVLGDYG RNVILNAGTG IMDHPSGPAS GVRAFFEALA
RIEAGESFDP ANLPEGALKQ AILEWG
