ID D3SFZ3_THISK Unreviewed; 473 AA. AC D3SFZ3; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {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|HAMAP-Rule:MF_01338}; GN Name=cbbL {ECO:0000256|HAMAP-Rule:MF_01338}; GN OrderedLocusNames=TK90_0858 {ECO:0000313|EMBL:ADC71373.1}; OS Thioalkalivibrio sp. (strain K90mix). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC71373.1, ECO:0000313|Proteomes:UP000009099}; RN [1] {ECO:0000313|Proteomes:UP000009099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.; RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADC71373.1, ECO:0000313|Proteomes:UP000009099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K90mix {ECO:0000313|EMBL:ADC71373.1, RC ECO:0000313|Proteomes:UP000009099}; RX PubMed=22675584; DOI=10.4056/sigs.2315092; RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H., RA Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.; RT "Complete genome sequence of Thioalkalivibrio sp. K90mix."; RL Stand. Genomic Sci. 5:341-355(2011). 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; CC Evidence={ECO:0000256|ARBA:ARBA00001067, ECO:0000256|HAMAP- CC Rule:MF_01338}; 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01338}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01338}; CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. CC {ECO:0000256|HAMAP-Rule:MF_01338}. 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; CP001905; ADC71373.1; -; Genomic_DNA. DR RefSeq; WP_012982269.1; NC_013889.1. DR AlphaFoldDB; D3SFZ3; -. DR STRING; 396595.TK90_0858; -. DR KEGG; tkm:TK90_0858; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_2_0_6; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000009099; Chromosome. 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-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 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}; 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}. FT DOMAIN 17..137 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 147..455 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 168 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 287 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 116 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 166 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 170 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 194 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 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 372 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 327 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 194 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 473 AA; 52788 MW; 7773541EE3964C71 CRC64; MAAKKYSAGV KDYRETYWMP EYMPLDTDLL ACFKITPQPG IDREEAAAAV AAESSTGTWT TVWTDLLTDM DYYKGRAYSI EDVPGDDESF YAFIAYPIDL FEEGSMVNVF TSLVGNVFGF KAIRALRLED VRFPMAYVKT CGGPPSGIQV ERDKLNKYGR PMLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN SQPFMRWRDR FEFVQEATEK AEAETGERKG HYLNVTAPTP EEMYKRAEFA KEIGAPIIMH DYITGGFCAN TGLANWCRDN GVLLHIHRAM HAVLDRHPKH GIHFRVLAKI LRLSGGDHLH TGTVVGKLEG DRAATLGWID LLRESFIPED RSRGIFFDQD WGSMPGVFAV ASGGIHVWHM PALVSIFGDD SVLQFGGGTL GHPWGNAPGA AANRVALEAC VQARNEGRDI EKEGKDILTQ AAQHSPELKI AMETWKEIKF EFDTVDKLDT QHK //