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Database: UniProt
Entry: A7Y492_9CYAN
LinkDB: A7Y492_9CYAN
Original site: A7Y492_9CYAN 
ID   A7Y492_9CYAN            Unreviewed;       412 AA.
AC   A7Y492;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:ABV04330.1};
OS   Thermoleptolyngbya oregonensis PCC 8501.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oculatellales; Oculatellaceae;
OC   Thermoleptolyngbya.
OX   NCBI_TaxID=561163 {ECO:0000313|EMBL:ABV04330.1};
RN   [1] {ECO:0000313|EMBL:ABV04330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OH-1-p Cl 1 {ECO:0000313|EMBL:ABV04330.1};
RA   Kroliczewski J., Szczepaniak A.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00001067};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|ARBA:ARBA00023587}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; EU119380; ABV04330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7Y492; -.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08212; RuBisCO_large_I; 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   InterPro; IPR020888; RuBisCO_lsuI.
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   Bacterial microcompartment {ECO:0000256|ARBA:ARBA00024446};
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Carboxysome {ECO:0000256|ARBA:ARBA00023669};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
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..399
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:ABV04330.1"
SQ   SEQUENCE   412 AA;  46195 MW;  E713132AF5C6E1B1 CRC64;
     GTWTTVWTDL LTDLDRYKGR CYDIEPVRGE DNQFIAYIAY PLDLFEEGSV TNMLTSIVGN
     VFGFKALKAL RLEDLRIPVA YLKTFQGPPH GIQVERDKLN KYGRPLLGCT IKPKLGLSAK
     NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFTFVAE AIHKAQAETG EIKGHYLNVT
     SATCEEMLKR AEYAKELGMP IIMHDFLTAG FTANTTLSKW CRDNGLLLHI HRAMHAVIDR
     RKNHGMHFRV LAKCLRMSGG DHIHTGTVVG KLEGDKAVTL GFVDLLRENY IERDPSKGIY
     FTQDWASMPG VMAVASGGIH VWHMPALVEI FGDDAVLQFG GGTLGHPWGN APGATANRVA
     LEACLQARNE GRDLMREGGD IIREACRWSP ELATACELWK EIKFEFEAVD TV
//
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