ID B7GLD0_ANOFW Unreviewed; 406 AA.
AC B7GLD0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000256|HAMAP-Rule:MF_01679};
DE Short=DK-MTP-1-P enolase {ECO:0000256|HAMAP-Rule:MF_01679};
DE EC=5.3.2.5 {ECO:0000256|HAMAP-Rule:MF_01679};
DE AltName: Full=RuBisCO-like protein {ECO:0000256|HAMAP-Rule:MF_01679};
DE Short=RLP {ECO:0000256|HAMAP-Rule:MF_01679};
GN Name=mtnW {ECO:0000256|HAMAP-Rule:MF_01679};
GN OrderedLocusNames=Aflv_1997 {ECO:0000313|EMBL:ACJ34356.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34356.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ34356.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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:0000256|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:0000256|HAMAP-Rule:MF_01679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01679};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01679}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01679}.
CC -!- MISCELLANEOUS: Has no RuBP-carboxylation activity. {ECO:0000256|HAMAP-
CC Rule:MF_01679}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01679}.
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DR EMBL; CP000922; ACJ34356.1; -; Genomic_DNA.
DR RefSeq; WP_012575543.1; NC_011567.1.
DR AlphaFoldDB; B7GLD0; -.
DR STRING; 491915.Aflv_1997; -.
DR GeneID; 7038249; -.
DR KEGG; afl:Aflv_1997; -.
DR PATRIC; fig|491915.6.peg.2049; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_9; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000000742; 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; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR NCBIfam; TIGR03332; salvage_mtnW; 1.
DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 2.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01679};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01679};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01679};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01679};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_01679}; Reference proteome {ECO:0000313|Proteomes:UP000000742}.
FT DOMAIN 124..293
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT DOMAIN 326..403
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 171..174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT BINDING 356..357
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT MOD_RES 171
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
SQ SEQUENCE 406 AA; 44201 MW; 2FA6D6BC832B63DC CRC64;
MITATYLIHD DKDLAKKAEG IALGLTVGSW TDLPQLEQEQ LKKHKGVVEA IEQLEEDERI
NTYVGKRLKR ALVRISYPSV NFSADFPAIL TTTFGKLSLD GTIKLVDLTF SDELKRAFPG
PRFGIDGIRE KLGVFDRPLV MSIFKAVIGR DLQYVTEQLK QQALGGVDLV KDDEILFDND
LTPFEKRIVA GKQALQEVYE QTGHRTLYAV NLTGKTFELK DKAKRAAELG ADVLLFNVFT
YGLDVLQALR EDDDIRLPIM AHPSFSGAIA SSHVYGVSYA LLLGKLLRMA GADFSLFPSP
YGSVALAKDE TLAIAHELTK EEPFLRTFPV PSAGIHPGLV PLLVRDFGID SVINAGGGVH
GHPSGAIGGG QAFRAAVDAV LAGRSLYDAA KENEPLQQAL DLWGGA
//
