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Database: UniProt
Entry: A0A0Q3WZL0_9BACI
LinkDB: A0A0Q3WZL0_9BACI
Original site: A0A0Q3WZL0_9BACI 
ID   A0A0Q3WZL0_9BACI        Unreviewed;       403 AA.
AC   A0A0Q3WZL0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:KQL54842.1};
GN   ORFNames=AN964_15885 {ECO:0000313|EMBL:KQL54842.1};
OS   Heyndrickxia shackletonii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL54842.1, ECO:0000313|Proteomes:UP000051888};
RN   [1] {ECO:0000313|EMBL:KQL54842.1, ECO:0000313|Proteomes:UP000051888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL54842.1,
RC   ECO:0000313|Proteomes:UP000051888};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQL54842.1}.
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DR   EMBL; LJJC01000004; KQL54842.1; -; Genomic_DNA.
DR   RefSeq; WP_055740626.1; NZ_LJJC01000004.1.
DR   AlphaFoldDB; A0A0Q3WZL0; -.
DR   STRING; 157838.AN964_15885; -.
DR   PATRIC; fig|157838.3.peg.3508; -.
DR   OrthoDB; 9770811at2; -.
DR   UniPathway; UPA00904; UER00876.
DR   Proteomes; UP000051888; Unassembled WGS sequence.
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; 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:UP000051888}.
FT   DOMAIN          2..93
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          120..399
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         167..170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         167
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         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         170
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   BINDING         352..353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
FT   MOD_RES         167
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01679"
SQ   SEQUENCE   403 AA;  44126 MW;  170D03F720E848FF CRC64;
     MSEVIATYSI YGKPKTFDKK AEDIALGLTI GSWTNLPIIE QDQLKKHKGR VISVEEIKTD
     SEENAKATIK IAYPSANFTP DLPAILTTVF GKLSLDGKVR LVDLELEGDI TKYFKGPRFG
     IHGIREKLNI FDRPLLMSIF KGVIGRDIPF LEKQLRNQAL GGVDLVKDDE ILFDLESAPF
     EKRIEMGRRV LDDVFQETGN RTLYAVNLTG RTLELRDKAR KARELGADLL LFNVFTYGLD
     ALQQLREDDE IGLPLMAHPA YSGAITQSKE YGVSHSLLLG KLLRLAGADF SLFPSPYGSV
     ALEKNAALSI GKALTEESFV KTTFPVPSAG IHPGLVPLLY QDFGLDSVIN AGGGIHGHPE
     GAIGGGKAFR QAIQAVLQNQ SLEDAASQFS ELRTALELWG AAK
//
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