ID F5BVW5_9MARC Unreviewed; 450 AA.
AC F5BVW5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 22-FEB-2023, entry version 32.
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:AEB33297.1};
OS Lepidozia bisbifida.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Jungermanniopsida; Jungermanniidae; Jungermanniales; Lophocoleineae;
OC Lepidoziaceae; Lepidozioideae; Lepidozia.
OX NCBI_TaxID=989927 {ECO:0000313|EMBL:AEB33297.1};
RN [1] {ECO:0000313|EMBL:AEB33297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EC43O {ECO:0000313|EMBL:AEB33297.1};
RX PubMed=21316477; DOI=10.1016/j.ympev.2011.02.006;
RA Cooper E.D., Shaw A.J., Shaw B., Henwood M.J., Heslewood M.M., Brown E.A.;
RT "A multi-locus molecular phylogeny of the Lepidoziaceae: Laying the
RT foundations for a stable classification.";
RL Mol. Phylogenet. Evol. 59:489-509(2011).
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 -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR EMBL; JF316305; AEB33297.1; -; Genomic_DNA.
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 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 3..119
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 129..437
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:AEB33297.1"
SQ SEQUENCE 450 AA; 49669 MW; 0FF2F236548A4438 CRC64;
TPXYETKATD ILAAFRMTPQ PGVPPEEAGA AVAAESSTGT WTTVWTDGLT SLDRYKGRCY
DIEPVAGEEN QYIAYVAYPL DLFEEGSVTN LFTSIVGNVS GFKALRALRL EDLRIPPAYV
KTFQGPPHGI QVERDKLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN
VNSQPFMRWR DRFLFVAEAL FKSQAETGEI KGHYLNATAG TSEEMMKRAA CARELGVPIV
MHDYLTGGFT ANTSLAHYCR DNGLLLHIHR AMHAVIDRQK NHGMHFRVLA KALRLSGGDH
IHAGTVVGKL EGERDVTLGF VDLLRDDYIE KDRSRGIYFT QDWVSLPGVL PVASGGIHVW
HMPALTEIFG DDSVLQFGGG TLGHPWGNAP GAVANRVALE ACVQARNEGR DLAREGNEVI
REAAKWSPDL AAACEVWKEI KFEYETIDTL
//
