ID F6LQM1_9BACT Unreviewed; 206 AA.
AC F6LQM1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit form IA {ECO:0000313|EMBL:AEE89930.1};
DE EC=4.1.1.39 {ECO:0000313|EMBL:AEE89930.1};
DE Flags: Fragment;
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AEE89930.1};
RN [1] {ECO:0000313|EMBL:AEE89930.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22092659; DOI=10.1111/j.1574-6941.2011.01246.x;
RA Alfreider A., Schirmer M., Vogt C.;
RT "Diversity and expression of different forms of RubisCO genes in polluted
RT groundwater under different redox conditions.";
RL FEMS Microbiol. Ecol. 79:649-660(2012).
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; JF414950; AEE89930.1; -; Genomic_DNA.
DR AlphaFoldDB; F6LQM1; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
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 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 Lyase {ECO:0000313|EMBL:AEE89930.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..81
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 91..206
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEE89930.1"
FT NON_TER 206
FT /evidence="ECO:0000313|EMBL:AEE89930.1"
SQ SEQUENCE 206 AA; 23505 MW; 726B4DAB405A2513 CRC64;
GTWTTVWTDL LTDLDYYKGR AYRIEDVPGD DTCFYAFVAY PIDLFEEGSV VNVMTSLVGN
VFGFKALRAL RLEDVRFPIA YVKTCGGPPH GIQVERDIMN KYGRPLLGCT IKPKLGLSAK
NYGRAVYECL RGGLDFTKDD ENVNSQPFMR WKQRFDFVQE ATEKAQRETG ERKGHYLNVT
APTPEEMYKR AEYAKSIGAP IIMHDY
//