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
//