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Database: UniProt
Entry: Q6XAQ8_9SYNE
LinkDB: Q6XAQ8_9SYNE
Original site: Q6XAQ8_9SYNE 
ID   Q6XAQ8_9SYNE            Unreviewed;       169 AA.
AC   Q6XAQ8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   28-JUN-2023, entry version 58.
DE   SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit {ECO:0000313|EMBL:AAP93949.1};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:AAP93949.1};
OS   Synechococcus sp. CB0201.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=232352 {ECO:0000313|EMBL:AAP93949.1};
RN   [1] {ECO:0000313|EMBL:AAP93949.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB0201 {ECO:0000313|EMBL:AAP93949.1};
RA   Chen F., Wang K., Bachoon D., Lu J., Lau S., Campbell L.;
RT   "Phylogenetic affiliation of marine Synechococcus spp. revealed by
RT   ribulose-1,5-bisphophate carboxylase/oxygenase large subunit gene
RT   sequences.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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; AY244819; AAP93949.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6XAQ8; -.
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   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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          2..102
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          112..169
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:AAP93949.1"
FT   NON_TER         169
FT                   /evidence="ECO:0000313|EMBL:AAP93949.1"
SQ   SEQUENCE   169 AA;  18857 MW;  67D263E81845BF7E CRC64;
     TGQEGVPKEE VAAAVAAESS TGTWSTVWSE LLTDLDFYKG RCYRIEDVPG DKESFYAFIA
     YPLDLFEEGS ITNVLTSLVG NVFGFKALRH LRLEDIRFPI AFIKSCYGPP NGIQVERDRM
     NKYGRPLLGC TIKPKLGLSG KNYGRVVYEC LRGGLDFTKD DENINSPPF
//
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