ID Q9TME7_9PHAE Unreviewed; 488 AA. AC Q9TME7; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-DEC-2019, entry version 104. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338}; DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; GN Name=rbcL {ECO:0000313|EMBL:BAA86087.1}; GN Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338}; GN ORFNames=Petal_109 {ECO:0000313|EMBL:AXC47209.1}; OS Endarachne binghamiae. OG Plastid {ECO:0000313|EMBL:BAA86087.1}. OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Scytosiphonaceae; Endarachne. OX NCBI_TaxID=698476 {ECO:0000313|EMBL:BAA86087.1}; RN [1] {ECO:0000313|EMBL:BAA86087.1} RP NUCLEOTIDE SEQUENCE. RA Kogame K., Horiguchi T., Masuda M.; RT "Phylogeny of the order Scytosiphonales (Phaeophyceae) based on DNA RT sequences of rbcL, partial rbcS and partial LSU nrDNA."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAJ78329.1} RP NUCLEOTIDE SEQUENCE. RA Kogame K., Kurihara A., Cho G.Y., Lee K.M., Sherwood A.R., Boo S.M.; RT "Petalonia tatewakii sp. nov. (Scytosiphonaceae, Phaeophyceae) from the RT Hawaiian Islands. Phycologia."; RL Phycologia 50:563-573(2011). RN [3] {ECO:0000313|EMBL:BAO56985.1} RP NUCLEOTIDE SEQUENCE. RA Matsumoto K., Ichihara K., Shimada S.; RT "Taxonomic reinvestigation of Petalonia (Phaeophyceae, Ectocarpales) in RT southeast of Honshu, Japan, with a description of Petalonia tenuis sp. RT nov."; RL Phycologia 53:127-136(2014). RN [4] {ECO:0000313|EMBL:AXC47209.1} RP NUCLEOTIDE SEQUENCE. RA Choi J.W., Louis G., Koki N., Asuka A., Eiichi S., Yoon H.S.; RT "Petalonia binghamiae, Cladosiphon okamuranus, Scytosiphon lomentaria RT plastid genomes."; RL Submitted (JUL-2017) 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. Both reactions occur simultaneously and in competition at CC the same active site. {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; Evidence={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|HAMAP-Rule:MF_01338, CC 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 CC {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|HAMAP-Rule:MF_01338}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}. 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; MF460360; AXC47209.1; -; Genomic_DNA. DR EMBL; AB022244; BAA86087.1; -; Genomic_DNA. DR EMBL; AB578992; BAJ78329.1; -; Genomic_DNA. DR EMBL; AB578993; BAJ78330.1; -; Genomic_DNA. DR EMBL; AB860185; BAO56985.1; -; Genomic_DNA. DR EMBL; AB860186; BAO56986.1; -; Genomic_DNA. DR EMBL; AB871992; BAO56994.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR CDD; cd08212; RuBisCO_large_I; 1. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 1. DR SUPFAM; SSF51649; SSF51649; 1. DR SUPFAM; SSF54966; SSF54966; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:BAA86087.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Photorespiration {ECO:0000256|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000313|EMBL:BAA86087.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 260..280 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 28..148 FT /note="RuBisCO_large_N" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 158..465 FT /note="RuBisCO_large" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 179 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 297 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 205 FT /note="Magnesium; via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 207 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 208 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 127 FT /note="Substrate; in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 177 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 181 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 298 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 330 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 382 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 337 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 205 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 488 AA; 53967 MW; E441E0E64536349B CRC64; MPEDVQNRTR IKSERYESGV IPYAKMGYWD ADYNVKETDI LALFRITPQP GVDPVEAAAA VAGESSTATW TVVWTDLLTA CDIYRAKAYR VDPVPGTSDQ FFAYIAYECD LFEEGSLANL TASIIGNVFG FKAVKALRLE DMRIPYAYLK TFQGPATGVV VERERLDKFG RPLLGATVKP KLGLSGKNYG RVVYEGLTGG LDFLKDDENI NSQPFMRWKE RFLYCMEGVN RAAAATGEVK GSYLNITAAT VEQMYERAEY AHSIGSVIVM IDLVIGYTAI QSMAIWARKY EMILHLHRAG NSTYARQKNH GINFRVICKW MRMCGVDHIH AGTVVGKLEG DPLMVKGFYN SLLLTHLKIN LAEGLFFDMD WAALRKCVPV ASGGIHCGQM HQLLYYLGDD VVLQFGGGTI GHPDGIQSGA TANRVALESM VLARNEGRDY VGEGPEILRK AASTCGPLKA ALDLWKDITF DYTSTDTPDF VEVATGSR //