ID C0ZL40_BREBN Unreviewed; 404 AA.
AC C0ZL40;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000313|EMBL:BAH45867.1};
DE EC=5.3.2.- {ECO:0000313|EMBL:BAH45867.1};
GN Name=mtnW {ECO:0000313|EMBL:BAH45867.1};
GN Synonyms=ykrW {ECO:0000313|EMBL:BAH45867.1};
GN OrderedLocusNames=BBR47_48900 {ECO:0000313|EMBL:BAH45867.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH45867.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH45867.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU003834}.
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DR EMBL; AP008955; BAH45867.1; -; Genomic_DNA.
DR RefSeq; WP_015893122.1; NC_012491.1.
DR AlphaFoldDB; C0ZL40; -.
DR STRING; 358681.BBR47_48900; -.
DR KEGG; bbe:BBR47_48900; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OMA; IHGHPDG; -.
DR Proteomes; UP000001877; Chromosome.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:InterPro.
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 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};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAH45867.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000001877}.
FT DOMAIN 6..110
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 120..400
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 404 AA; 43064 MW; 1911DB83F2F03EFA CRC64;
MSEQRILVTY LTQAKDLNKK AQAIAVGMTV GSWTDLPLAK QAMLAPYLGE AVSATPIATL
ENGETRGLIT VSYPTRNFTA DIPSLLTGIF GKLSMDGKIK LVDIVFPESF LQAFPGPKFG
IDGLRERLGA HNRPLLMSIF KSCLGLPFDD LKTQFRAQAL GGVDLVKDDE IFFADDRAPF
IERIKAFKQI AQETEAETGK PVLYAANLTG PVHELNEKAK RAVEAGADCL LFNVLAFGFD
ALHRLAADPD VHVPIMAHPA LAGAYYPSPD YGIATPLLLG TLMRVAGADL VLFPSPYGNV
ALDKTEALQL AKHLTDPLNG VRRSFPVPSA GIHPGLVPQL YQDFGLDQIV NAGGGIHGHP
GGATAGAKAF VAAIEAVTAG RTLEEASSES QELAIALEKW GGAR
//