ID Q85V61_9BRYO Unreviewed; 475 AA.
AC Q85V61;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 22-FEB-2023, entry version 106.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|HAMAP-Rule:MF_01338};
GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338,
GN ECO:0000313|EMBL:BAC76090.1};
OS Wijkia concavifolia.
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAC76090.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Bryidae; Hypnanae; Hypnales; Pylaisiadelphaceae;
OC Wijkia.
OX NCBI_TaxID=213177 {ECO:0000313|EMBL:BAC76090.1};
RN [1] {ECO:0000313|EMBL:BAC76090.1}
RP NUCLEOTIDE SEQUENCE.
RA Tsubota H., Arikawa T., Akiyama H., De Luna E., Gonzalez D., Higuchi M.,
RA Deguchi H.;
RT "Molecular phylogeny of hypnobryalean mosses as inferred from a large-scale
RT dataset of chloroplast rbcL, with special reference to the Hypnaceae and
RT possibly related families.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAD98511.1}
RP NUCLEOTIDE SEQUENCE.
RA Tsubota H., De Luna E., Gonzalez D., Ignatov M.S., Deguchi H.;
RT "Molecular phylogenetic and ordinal relationships of mosses based on
RT analysis of a large-scale data set of rbcL sequences.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site.
CC {ECO:0000256|HAMAP-Rule:MF_01338}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01338, 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|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01338,
CC ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01338,
CC ECO:0000256|RuleBase:RU000302};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204, ECO:0000256|HAMAP-
CC Rule:MF_01338}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
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DR EMBL; AB095271; BAC76090.1; -; Genomic_DNA.
DR EMBL; AB194963; BAD98511.1; -; Genomic_DNA.
DR AlphaFoldDB; Q85V61; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:BAC76090.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01338}; Methylation {ECO:0000256|HAMAP-Rule:MF_01338};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01338,
KW ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:BAC76090.1}.
FT DOMAIN 24..144
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 154..462
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 14
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
SQ SEQUENCE 475 AA; 52595 MW; 6A98C1821B893F18 CRC64;
MSPQTETKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYDLEAV PGEENQYIAY VAYPLDLFEE GSVTNLSTSI
VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKSQA ETGEIKGHYL
NATAGTSEEM LKRAQFAREL GMPIIMHDYL TGGFTANTSL AHYARDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERQ VTLGFVDLPR DDYIEKDRSR
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVQA RNEGRDLARE GNEVIREATK WSPELAAACE VWKEIKFEFD TIDTI
//
