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Database: UniProt/TrEMBL
Entry: A0A1X9M7X8_9BACI
LinkDB: A0A1X9M7X8_9BACI
Original site: A0A1X9M7X8_9BACI 
ID   A0A1X9M7X8_9BACI        Unreviewed;       397 AA.
AC   A0A1X9M7X8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ECO:0000313|EMBL:ARK29517.1};
GN   ORFNames=BkAM31D_06395 {ECO:0000313|EMBL:ARK29517.1};
OS   Halalkalibacter krulwichiae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK29517.1, ECO:0000313|Proteomes:UP000193006};
RN   [1] {ECO:0000313|EMBL:ARK29517.1, ECO:0000313|Proteomes:UP000193006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM31D {ECO:0000313|EMBL:ARK29517.1,
RC   ECO:0000313|Proteomes:UP000193006};
RA   Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT   "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL   Submitted (APR-2017) 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: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; CP020814; ARK29517.1; -; Genomic_DNA.
DR   RefSeq; WP_066154094.1; NZ_CP020814.1.
DR   AlphaFoldDB; A0A1X9M7X8; -.
DR   STRING; 199441.BkAM31D_06395; -.
DR   KEGG; bkw:BkAM31D_06395; -.
DR   UniPathway; UPA00904; UER00876.
DR   Proteomes; UP000193006; 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   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; IPR017443; RuBisCO_lsu_fd_N.
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; 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; 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:UP000193006}.
FT   DOMAIN          5..89
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          116..394
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         162..165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         162
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         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         347..348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   MOD_RES         162
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
SQ   SEQUENCE   397 AA;  42555 MW;  0890E24E21F2BCC6 CRC64;
     MSEVQATYLL EAEQANLNKK AEAIALGLTV GSWTNLPAVE QEQLAKHKGR VVEAKMIAEG
     KAIITVGYPS ANFSNDLPAV LTTTFGKFSL DGKVKLLDLT FSDDIKHGYP GPKFGLEGIR
     QLTNTYDRPL LMSIFKGVIG RDLHSLKEQM KAQALGGIDI VKDDEILFEN DLTPLEKRIP
     VCQEALRESY EITGKRTLHA VNLTGKTMEL KENAYKAVEL GADLLLFNTF AYGLDVMQAL
     AEDPNIPLPI MAHPAFSGTM ISSPDYGLAP GLLLGKLARM AGADLVLFPS PYGSVAMAKE
     ETQAIAKHLT EDDQFKKAFP VPSAGIHPGL TPKLIADFGV DSIINAGGGI HGHPGGAAAG
     GRAFVQAIDA VLANQPLHDA AKDYEELAKA LELWGGE
//
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