ID Q5VAS2_9MARC Unreviewed; 436 AA.
AC Q5VAS2;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 65.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|RuleBase:RU000302};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|RuleBase:RU000302};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:AAT45776.1};
OS Diplasiolejeunea involuta.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAT45776.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Jungermanniopsida; Jungermanniidae; Porellales; Jubulineae; Lejeuneaceae;
OC Lejeuneoideae; Lejeuneeae; Cololejeuneinae; Diplasiolejeunea.
OX NCBI_TaxID=280572 {ECO:0000313|EMBL:AAT45776.1};
RN [1] {ECO:0000313|EMBL:AAT45776.1}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R., Gradstein S.R., Heinrichs J., Groth H., Ilkiu-Borges A.-L.,
RA Hartmann F.A.;
RT "Phylogeny of Lejeuneaceae: A cladistic analysis of chloroplast gene rbcL
RT sequences and morphology with preliminary comments on the mitochondrial
RT nad4-2 spacer region.";
RL (In) Goffinet B., Hollowell V., Magill R. (eds.);
RL MOLECULAR SYSTEMATICS OF BRYOPHYTES: MONOGRAPHS IN SYSTEMATIC BOTANY FROM
RL THE MISSOURI BOTANICAL GARDEN SERIES (VOL. 98), pp.189-202, Missouri
RL Botanical Garden Press, St. Louis, MO, USA (2004).
RN [2] {ECO:0000313|EMBL:AAT45776.1}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R., Hartmann F.A.;
RL Submitted (FEB-2004) 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 ECO:0000256|RuleBase:RU000302};
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 ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR EMBL; AY548096; AAT45776.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VAS2; -.
DR GO; GO:0009507; C:chloroplast; 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: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 ECO:0000256|RuleBase:RU000302};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU000302};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:AAT45776.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000302};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000302};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000302};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238,
KW ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 7..127
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 137..423
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:AAT45776.1"
FT NON_TER 436
FT /evidence="ECO:0000313|EMBL:AAT45776.1"
SQ SEQUENCE 436 AA; 48280 MW; 6760B1C4D5B430ED CRC64;
KDYRLTYYTP DYQVKATDIL AAFRMTPQAG VPAEEAGAAV AAESSTGTWT TVWTDGLTSL
DRYKGRCYDI EPVRGEENQY IAYVAYPLDL FEEGSVTNLF TSIVGNVFGF KALRALRLED
LRIPPAYVKT FQGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL
DFTKDDENVN SQPFMRWRDR FLFVAEAIFK SQAETGEIKG HYLNATAGTC EEMIKRAQCA
RELGVPIIMH DYLTGGFTAN TSLAHYSRDN GLLLHIHRAM HAVIDRQKNH GMHFRVLAKA
LRLSGGDHIH AGTVVGKLEG EREVTLGFVD LLRDDYIEKD RSRGVYFTQD WVSLPGVLPV
ASGGIHVWHM PALTDIFGDD SVLQFGGGTL GHPWGNAPGA VANRVALEAC VQARNEGRSL
ADEGNEVIKE ALKWSP
//
