ID A0A4P8XU74_GUITH Unreviewed; 344 AA. AC A0A4P8XU74; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 14-DEC-2022, entry version 9. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302}; DE EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302}; DE Flags: Fragment; GN Name=rbcL {ECO:0000313|EMBL:QCT05629.1}; OS Guillardia theta (Cryptophyte) (Cryptomonas phi). OG Plastid {ECO:0000313|EMBL:QCT05629.1}. OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia. OX NCBI_TaxID=55529 {ECO:0000313|EMBL:QCT05629.1}; RN [1] {ECO:0000313|EMBL:QCT05629.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP327 {ECO:0000313|EMBL:QCT05629.1}; RX PubMed=31088271; DOI=.1098/rspb.2019.0655; RA Greenwold M.J., Cunningham B.R., Lachenmyer E.M., Pullman J.M., RA Richardson T.L., Dudycha J.L.; RT "Diversification of light capture ability was accompanied by the evolution RT of phycobiliproteins in cryptophyte algae."; RL Proc. R. Soc. B 286:20190655-20190655(2019). 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. CC {ECO:0000256|RuleBase:RU000302}. 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; MK818447; QCT05629.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4P8XU74; -. 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 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 Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 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}; 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|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QCT05629.1}. FT DOMAIN 9..129 FT /note="RuBisCO_large_N" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 139..341 FT /note="RuBisCO_large" FT /evidence="ECO:0000259|Pfam:PF00016" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QCT05629.1" FT NON_TER 344 FT /evidence="ECO:0000313|EMBL:QCT05629.1" SQ SEQUENCE 344 AA; 38325 MW; E2AA12E4C900C052 CRC64; VIPYAKMGYW DADYVIKDTD VLAMFRMTPQ KGVDPVECAA AIAGESSTAT WTVVWTDLLT ACDLYRAKAY RVDPVPGATD QYFAYIAYEL DLFEEGSLAN LTASIIGNVF GFKAVNALRL EDMRLPIAYL KTFQGPATGV IVERERLDKY GRPLLGATVK PKLGLSGKNY GRVVYEGLKG GLDFLKDDEN INSQPFMRWK ERFLFGIEGV NRAAAAAGEV KGHYFNVTAG TMEDMYERAE FCKEIGSVIC MIDLVIGYTA IQSMAIWARK NSMILHLHRA GNSTYSRQKT HGMNFRVICK WMRMAGVDHI HAGTVVGKLE GDPLMVKGFY NTLLETQTDV NLVQ //