ID RBL2_MAGSA Reviewed; 459 AA. AC Q2W3S5; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339}; DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339}; DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339}; GN Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339}; GN OrderedLocusNames=amb2696; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Magnetospirillaceae; Paramagnetospirillum. OX NCBI_TaxID=342108; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264; RX PubMed=16303747; DOI=10.1093/dnares/dsi002; RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.; RT "Complete genome sequence of the facultative anaerobic magnetotactic RT bacterium Magnetospirillum sp. strain AMB-1."; RL DNA Res. 12:157-166(2005). 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:0000255|HAMAP-Rule:MF_01339}. 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:0000255|HAMAP- CC Rule:MF_01339}; 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:0000255|HAMAP-Rule:MF_01339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01339}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01339}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01339}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a 'head-to-tail' conformation. In contrast to form I CC RuBisCO, the form II RuBisCO are composed solely of large subunits. CC {ECO:0000255|HAMAP-Rule:MF_01339}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01339}. 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; AP007255; BAE51500.1; -; Genomic_DNA. DR RefSeq; WP_011385076.1; NC_007626.1. DR AlphaFoldDB; Q2W3S5; -. DR SMR; Q2W3S5; -. DR STRING; 342108.amb2696; -. DR KEGG; mag:amb2696; -. DR HOGENOM; CLU_031450_3_1_5; -. DR OrthoDB; 9764279at2; -. DR Proteomes; UP000007058; 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-KW. DR CDD; cd08211; RuBisCO_large_II; 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_01339; RuBisCO_L_type2; 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; IPR020871; RuBisCO_lsuII. 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; 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; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; KW Monooxygenase; Oxidoreductase; Reference proteome. FT CHAIN 1..459 FT /note="Ribulose bisphosphate carboxylase" FT /id="PRO_0000251407" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT ACT_SITE 287 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 111 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 368 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT SITE 329 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT MOD_RES 191 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" SQ SEQUENCE 459 AA; 50349 MW; 3A16B2EE0C3BABBB CRC64; MDQSKRYVNL GLREADLIKG GRHVLCAYRM RPRPGHGYVE TAAHFAAESS TGTNVEVCTT DDFTRGVDAL VYEVDEAEGL MKIAYPVELF DRNIIDGKAM IASFLTLTVG NNQGMSDVEN AKMEDFYVPP DFLTLFDGPA RNIAHMWKVL GRPEVNGGMV VGTIIKPKLG LRPKPFADAC HQFWLGGDFI KNDEPQGNQV FAPFKDTMRL VADSMRRAQD ETGQAKLFSA NITADDPAEM IARGQFILDT FGENASHVAF LVDGFVAGPT AVTTCRRNFP DTFLHYHRAG HGAITSRQSK RGYSVLVHMK MARLLGASGI HTGTMGYGKM EGAPDEKVVA YMLERPTAEG PHYRQDWGDM RACTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHK DGPVAGALSL RQAHEAWMRG ISLVEYAQGH PELRGAFESF ASDADRLYPG WRDRLRIAA //