ID B7P0F3_9GENT Unreviewed; 430 AA.
AC B7P0F3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:ACK76570.1};
OS Haplophyton crooksii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae;
OC Aspidospermateae; Haplophyton.
OX NCBI_TaxID=141567 {ECO:0000313|EMBL:ACK76570.1};
RN [1] {ECO:0000313|EMBL:ACK76570.1}
RP NUCLEOTIDE SEQUENCE.
RA Simoes A.O., Livshultz T., Conti E., Endress M.E.;
RT "Phylogeny and systematics of the Rauvolfioideae (Apocynaceae) based on
RT molecular and morphological evidence.";
RL Ann. Mo. Bot. Gard. 94:268-297(2007).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272; Evidence={ECO:0000256|ARBA:ARBA00000537};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers. {ECO:0000256|ARBA:ARBA00025888}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR EMBL; DQ660647; ACK76570.1; -; Genomic_DNA.
DR AlphaFoldDB; B7P0F3; -.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 HAMAP; MF_01338; RuBisCO_L_type1; 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; SFLDG01052; RuBisCO; 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 Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238};
KW Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 1..111
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 121..429
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:ACK76570.1"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:ACK76570.1"
SQ SEQUENCE 430 AA; 47396 MW; 2A2A007FE7531305 CRC64;
TDILAAFRVT PQPGVPPEEA GAAVAAESST GTWTTVWTDG LTSLDRYKGR CYHIEPVPGE
EDQFIAYVAY PLDLFEEGSV TNMFTSIVGN VFGFKALRAL RLEDLRVPPA YIKTFQGPPH
GIQVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD ENVNSQPFMR
WRDRFLFCAE AIYKAQAETG EIKGHYLNAT AGTCEEMIKR AVCARELGVP IVMHDYLTGG
FTANTSLAHY CRDNGLLLHI HRAMHAVIDR QKNHGMHFRV LAKALRMSGG DHIHAGTVVG
KLEGERDITL GFVDLLRDDF VEKDRSRGIY FTQDWVSLPG VLPVASGGIH VWHMPALTEI
FGDDSVLQFG GGTLGHPWGN APGAVANRVA LEACVQARNE GRDLAVEGNE IIREASKWSP
ELAAACEIWK
//
