ID Q53DF2_9BRYO Unreviewed; 430 AA.
AC Q53DF2;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, 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:AAS98677.1};
OS Mesochaete taxiforme.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAS98677.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Bryidae; Bryanae; Rhizogoniales; Aulacomniaceae;
OC Mesochaete.
OX NCBI_TaxID=272284 {ECO:0000313|EMBL:AAS98677.1};
RN [1] {ECO:0000313|EMBL:AAS98677.1}
RP NUCLEOTIDE SEQUENCE.
RA Bell N.E., Newton A.E.;
RT "Systematic studies of non-hypnanaean pleurocarps: establishing a
RT phylogenetic framework for investigating the origins of pleurocarpy.";
RL (In) Goffinet, B., Hollowell, V.C. and Magill, R.E. (eds.);
RL MOLECULAR SYSTEMATICS OF BRYOPHYTES: MONOGRAPHS IN SYSTEMATIC BOTANY FROM
RL THE MISSOURI BOTANICAL GARDEN SERIES (VOL. 98), pp.290-319, Missouri
RL Botantical Garden, St. Louis, MO, USA (2004).
RN [2] {ECO:0000313|EMBL:AAS98677.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1600/0363644053661896;
RA Bell N.E., Newton A.E.;
RT "The paraphyly of Hypnodendron and the phylogeny of related non-hypnanaean
RT pleurocarpous mosses inferred from chloroplast and mitochondrial sequence
RT data.";
RL Syst. Bot. 30:34-51(2005).
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; AY524434; AAS98677.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53DF2; -.
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:AAS98677.1};
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, ECO:0000313|EMBL:AAS98677.1}.
FT DOMAIN 1..116
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 126..430
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:AAS98677.1"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:AAS98677.1"
SQ SEQUENCE 430 AA; 47486 MW; 5C493BA1DF6BF5AF CRC64;
YQTKETDILA AFRMTPQPGV PAEEAGAAVA AESSTGTWTT VWTDGLTSLD RYKGRCYDIE
AVPGEDNQYI AYVAYPLDLF EEGSVTNLFT SIVGNVFGFK ALRALRLEDL RIPPAYSKTF
QGPPHGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS
QPFMRWRDRF LFVDEALYKS QAETGEIKGH YLNATAGTCE EMMKRAQFAR ELGAPIVMHD
YLTGGFTANT TLAHYCRDNG LLLHIHRAMH AVIDRQKNHG MHFRVLAKAL RLSGGDHIHA
GTVVGKLEGE RQVTLGFVDL LRDDYIEKDR SRGIYFTQDW VSLPGVLPVA SGGIHVWHMP
ALTEIFGDDS VLQFGGGTLG HPWGNAPGAV ANRVAVEACV QARNEGRDLA REGNEIIREA
AKWSPELAAA
//
