ID A0A0U2W4Q9_9BACL Unreviewed; 420 AA.
AC A0A0U2W4Q9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000313|EMBL:ALS30195.1};
GN ORFNames=IJ21_48340 {ECO:0000313|EMBL:ALS30195.1};
OS Paenibacillus sp. 32O-W.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS30195.1, ECO:0000313|Proteomes:UP000059673};
RN [1] {ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS30195.1, ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|EMBL:ALS30195.1,
RC ECO:0000313|Proteomes:UP000059673};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU003834}.
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DR EMBL; CP013653; ALS30195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2W4Q9; -.
DR STRING; 1695218.IJ21_48340; -.
DR KEGG; pow:IJ21_48340; -.
DR PATRIC; fig|1695218.3.peg.5214; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000059673; Chromosome.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08207; RLP_NonPhot; 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; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
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; 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; SFLDS00014; RuBisCO; 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.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000059673}.
FT DOMAIN 4..129
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 139..417
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 420 AA; 45668 MW; 5A93FD97BEAE5E30 CRC64;
MHNERVIATY LIETPYPLEK AAEAMAGEQS TGTFIAVPGE TPELKAQHGA QIVGLEQIGE
YDRPSLPECY VPPGIDKPVY RRAIVKLSFP LHNFGPSLPN LLATVAGNLY ELREFSGLRL
TDLELPEAFA ARYPGPKFGI EGTRRLAGVH DRPIIGTIVK PSIGLPISEY GPLIRELAEA
GLDFVKDDEL CGDPPAAPFE QRVAAVMAEI ERAADRTGKK MMYAFNISGD IDEMRRRHDI
VAKAGGTCVM VSINSVGWAG VAHLRQYAEL PIHGHRNQWG AMTRYPLLGM SFTAYQKLCR
LAGVDHLHTN GLNSKFAESN ESVAQSIRDC LTPMFGGYTV MPVLSSAQWA GSAIPTYRAV
PTQDVIHLAG GGILAHPGGI AAGVRSMRQG WEAAVQGIEL DEYARSRPEL QAAIRTFGKK
//