ID A8DP56_THAPS Unreviewed; 490 AA. AC A8DP56; B8LER9; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 24-JAN-2024, entry version 92. 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:ABF60342.1}; GN Synonyms=RBL {ECO:0000313|EMBL:EED86158.1}; GN ORFNames=THAPSDRAFT_bd2088 {ECO:0000313|EMBL:EED86158.1}; OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana). OG Plastid; Chloroplast {ECO:0000313|EMBL:ABF60342.1}. OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales; OC Thalassiosiraceae; Thalassiosira. OX NCBI_TaxID=35128 {ECO:0000313|EMBL:ABF60342.1}; RN [1] {ECO:0000313|EMBL:EED86158.1, ECO:0000313|Proteomes:UP000001449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED86158.1}; RX PubMed=15459382; DOI=10.1126/science.1101156; RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D., RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A., RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C., RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M., RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W., RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M., RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A., RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A., RA Wilkerson F.P., Rokhsar D.S.; RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and RT metabolism."; RL Science 306:79-86(2004). RN [2] {ECO:0000313|EMBL:ABF60342.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NEPC709 {ECO:0000313|EMBL:ABF60342.1}; RX PubMed=17553708; DOI=10.1016/j.ympev.2007.03.024; RA Alverson A.J., Jansen R.K., Theriot E.C.; RT "Bridging the Rubicon: phylogenetic analysis reveals repeated colonizations RT of marine and fresh waters by thalassiosiroid diatoms."; RL Mol. Phylogenet. Evol. 45:193-210(2007). RN [3] {ECO:0000313|EMBL:EED86158.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED86158.1}; RX PubMed=18923393; DOI=10.1038/nature07410; RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A., RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T., RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P., RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C., RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D., RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G., RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J., RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A., RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L., RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A., RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R., RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., RA Grigoriev I.V.; RT "The Phaeodactylum genome reveals the evolutionary history of diatom RT genomes."; RL Nature 456:239-244(2008). RN [4] {ECO:0000313|EMBL:EED86158.1, ECO:0000313|Proteomes:UP000001449} RP GENOME REANNOTATION. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED86158.1}; RG Diatom Consortium; RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C., RA Schmutz J., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., RA Bruce D., Pitluck S., Rokhsar D., Armbrust V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:AEB91175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:AEB91175.1}; RA Theriot E.C., Ashworth M., Ruck E., Nakov T., Jansen R.K.; RT "A preliminary multigene phylogeny of the diatoms (Bacillariophyta): RT challenges for future research."; RL Plant Ecol Evol 143:278-296(2010). RN [6] {ECO:0000313|EMBL:AEB91175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:AEB91175.1}; RA Theriot E.C., Ashworth M., Ruck E.C., Nakov T., Jansen R.K.; RL Submitted (JAN-2011) 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. 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; DQ514784; ABF60342.1; -; Genomic_DNA. DR EMBL; HQ912419; AEB91175.1; -; Genomic_DNA. DR EMBL; DS999447; EED86158.1; -; Genomic_DNA. DR RefSeq; XP_002297518.1; XM_002297482.1. DR RefSeq; YP_874498.1; NC_008589.1. DR SMR; A8DP56; -. DR STRING; 35128.A8DP56; -. DR EnsemblProtists; EED86158; EED86158; THAPSDRAFT_bd2088. DR GeneID; 4524793; -. DR GeneID; 7447414; -. DR KEGG; tps:THAPSDRAFT_bd2088; -. DR HOGENOM; CLU_031450_2_0_1; -. DR OMA; IHGHPDG; -. DR Proteomes; UP000001449; Unassembled WGS sequence. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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 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:ABF60342.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302}; KW Membrane {ECO:0000256|SAM:Phobius}; 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:ABF60342.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001449}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 264..287 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 28..148 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 158..467 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:ABF60342.1" SQ SEQUENCE 490 AA; 54324 MW; A8FBC8583F358EBE CRC64; MSQSVSERTR IKSDRYESGV IPYAKMGYWD AAYTVKDTDV LALFRITPQP GVDPVEAAAA VAGESSTATW TVVWTDLLTA CERYRAKAYR VDPVPSATDQ YFAFIAYECD LFEEASLSNL TASIIGNVFG FKAISALRLE DMRIPHSYLK TFQGPATGIV VERERLNKYG TPLLGATVKP KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWRE RFLNCLEGIN RASAATGEVK GSYLNITAAT MEEVYKRAEY AKMIGSVIVM IDLVMGYTAI QSIAYWAREN DMLLHLHRAG NSTYARQKNH GINFRVICKW MRMSGVDHIH AGTVVGKLEG DPLMIKGFYD ILRLTELEVN LPFGIFFEMD WASLRRCMPV ASGGIHCGQM HQLIHYLGDD VVLQFGGGTI GHPDGIQAGA TANRVALEAM VLARNEGLDY FNQQVGPQIL RDAAKTCGPL QTALDLWKDI SFNYTSTDTA DFAETATANR //