ID Q95DI4_9MONI Unreviewed; 415 AA. AC Q95DI4; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 02-OCT-2024, entry version 85. 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:BAB69795.1}; OS Leptogramma gymnocarpa. OG Plastid; Chloroplast {ECO:0000313|EMBL:BAB69795.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Polypodiopsida; Polypodiidae; Polypodiales; Aspleniineae; Thelypteridaceae; OC Thelypteridoideae; Leptogramma. OX NCBI_TaxID=157681 {ECO:0000313|EMBL:BAB69795.1}; RN [1] {ECO:0000313|EMBL:BAB69795.1} RP NUCLEOTIDE SEQUENCE. RA Kakugawa-Yatabe Y., Murakami N.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAB69795.1} RP NUCLEOTIDE SEQUENCE. RA Yatabe Y., Murakami M.; RT "Cryptic Species in Stegnogramma pozoi."; RL Submitted (OCT-2001) 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|ARBA:ARBA00025664}. 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 disulfide-linked. The disulfide link is formed within the large subunit CC homodimers. {ECO:0000256|ARBA:ARBA00025888}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB059745; BAB69795.1; -; Genomic_DNA. DR AlphaFoldDB; Q95DI4; -. 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 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 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 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:BAB69795.1}; 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:BAB69795.1}. 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..414 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:BAB69795.1" FT NON_TER 415 FT /evidence="ECO:0000313|EMBL:BAB69795.1" SQ SEQUENCE 415 AA; 46086 MW; D354DBDA3FE04C8B CRC64; KDYRLTYYTP EYKTKDTDIL AAFRMTPQPG VPAEEAGAAV AAESSTGTWT TVWTDGLTSL DRYKGRCYDI EPVAGEENQY IAYVAYPLDL FEEGSVTNLF TSIVGNVFGF KALRALRLED LRIPPAYSKT FMGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN SQPFMRWRDR FLFVAEALFK SQAETGEIKG HYLNATAGTC EEMLKRAVFA RELGAPIVMH DYLTGGFTAN TSLAFYCRDN GLLLHIHRAM HAVIDRQRNH GMHFRVLAKA LRMSGGDHIH AGTVVGKLEG EREVTLGFVD LLRDDYIEKD RSRGIYFTQD WVSMPGVFPV ASGGIHVWHM PALTEIFGDD SVLQFGGGTL GHPWGNAPGA VANRVALEAC VQARN //