ID A4K825_9BRYO Unreviewed; 437 AA.
AC A4K825;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 22-FEB-2023, entry version 51.
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:ABE76804.1};
OS Fissidens taxifolius.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ABE76804.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Dicranidae; Dicranales; Fissidentaceae; Fissidens.
OX NCBI_TaxID=52983 {ECO:0000313|EMBL:ABE76804.1};
RN [1] {ECO:0000313|EMBL:ABE76804.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N157 {ECO:0000313|EMBL:ABE76804.1};
RA Newton A.E., Wikstrom N., Bell N.E., Forrest L.L., Ignatov M.S.;
RT "Dating the diversification of the pleurocarpous mosses.";
RL (In) Newton A.E., Tangney R.S. (eds.);
RL PLEUROCARPOUS MOSSES: SYSTEMATICS AND EVOLUTION, pp.0-0, CRC Press (2006).
RN [2] {ECO:0000313|EMBL:ABE76804.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N157 {ECO:0000313|EMBL:ABE76804.1};
RA Newton A.E., Wikstrom N., Bell N.E., Forrest L.L., Ignatov M.S.;
RL Submitted (MAR-2006) 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; DQ463104; ABE76804.1; -; Genomic_DNA.
DR AlphaFoldDB; A4K825; -.
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:ABE76804.1};
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:ABE76804.1}.
FT DOMAIN 12..132
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 142..428
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:ABE76804.1"
FT NON_TER 437
FT /evidence="ECO:0000313|EMBL:ABE76804.1"
SQ SEQUENCE 437 AA; 48469 MW; 2C7894EC6C0412EF CRC64;
FKAGVKDYRL TYYTPNYQTL ETDILAAFRM TPQPGVPPEE AGAAVAAESS TGTWTTVWTD
GLTSLDRYKG RCYDIEAVPG EENQYIAYVA YPLDLFEEGS VTNLFTSIVG NVFGFKALRA
LRLEDLRIPP AYSKTFQGPP HGIQVERDKL NKYGRPLLGC TIKPKLGLSA KNYGRAVYEC
LRGGLDFTKD DENVNSQPFM RWRDRFLFVA EAIYKSQAET GEIKGHYLNA TAGTCEEMLK
RAQFARELGV PIVMHDYLTG GFTANTTLAH YCRDNGLLLH IHRAMHAVID RQKNHGMHFR
VLAKALRLSG GDHIHAGTVV GKLEGERQVT LGFVDLLRDD YIEKDRSRGI YFTQDWVSLP
GILPVASGGI HVWHMPALTE IFGDDSVLQF GGGTLGHPWG NAPGAVANRV ALEACVQARN
EGRDLAREGN EIIREAA
//
