ID RBL2_RHORU Reviewed; 466 AA. AC P04718; P19365; P72313; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 24-JAN-2024, entry version 142. DE RecName: Full=Ribulose bisphosphate carboxylase; DE Short=RuBisCO; DE EC=4.1.1.39; GN Name=cbbM; Synonyms=cbbL2, rbpL; OS Rhodospirillum rubrum. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1085; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Nargang F., McIntosh L., Somerville C.R.; RT "Nucleotide sequence of the ribulosebisphosphate carboxylase gene from RT Rhodospirillum rubrum."; RL Mol. Gen. Genet. 193:220-224(1984). RN [2] RP PROTEIN SEQUENCE OF 314-337. RX PubMed=6404301; DOI=10.1021/bi00275a028; RA Fraij B., Hartman F.C.; RT "Isolation and sequencing of an active-site peptide from Rhodospirillum RT rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling RT with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate."; RL Biochemistry 22:1515-1520(1983). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT. RX PubMed=16453738; DOI=10.1002/j.1460-2075.1986.tb04662.x; RA Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G.; RT "Three-dimensional structure of ribulose-1,5-bisphosphate RT carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."; RL EMBO J. 5:3409-3415(1986). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), COFACTOR, AND SUBUNIT. RA Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., RA Braenden C.-I., Lorimer G.H.; RT "Crystal structure of the active site of ribulose-bisphosphate RT carboxylase."; RL Nature 337:229-234(1989). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT. RX PubMed=2107319; DOI=10.1016/0022-2836(90)90088-4; RA Schneider G., Lindqvist Y., Lundqvist T.; RT "Crystallographic refinement and structure of ribulose-1,5-bisphosphate RT carboxylase from Rhodospirillum rubrum at 1.7-A resolution."; RL J. Mol. Biol. 211:989-1008(1990). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF ACTIVATED ENZYME, COFACTOR, RP SUBUNIT, AND CARBOXYLATION AT LYS-191. RX PubMed=1899197; DOI=10.1021/bi00218a004; RA Lundqvist T., Schneider G.; RT "Crystal structure of the ternary complex of ribulose-1,5-bisphosphate RT carboxylase, Mg(II), and activator CO2 at 2.3-A resolution."; RL Biochemistry 30:904-908(1991). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT ASN-193, FUNCTION, ACTIVE RP SITE, SUBUNIT, AND MUTAGENESIS OF ASP-193. RX PubMed=1606957; DOI=10.1111/j.1432-1033.1992.tb16979.x; RA Soderlind E., Schneider G., Gutteridge S.; RT "Substitution of ASP193 to ASN at the active site of ribulose-1,5- RT bisphosphate carboxylase results in conformational changes."; RL Eur. J. Biochem. 206:729-735(1992). 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. 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:1899197, CC ECO:0000269|Ref.4}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1606957, CC ECO:0000269|PubMed:16453738, ECO:0000269|PubMed:1899197, CC ECO:0000269|PubMed:2107319, ECO:0000269|Ref.4}. 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 (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II CC subfamily. {ECO:0000305}. 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; X00286; CAA25080.1; -; Genomic_DNA. DR PIR; S07295; S07295. DR PDB; 1RBA; X-ray; 2.60 A; A/B=1-466. DR PDB; 1RUS; X-ray; 2.90 A; A/B=1-466. DR PDB; 2RUS; X-ray; 2.30 A; A/B=1-466. DR PDB; 5HQM; X-ray; 1.95 A; A/B=17-303, A/B=456-466. DR PDB; 5RUB; X-ray; 1.70 A; A/B=1-466. DR PDB; 9RUB; X-ray; 2.60 A; A/B=1-466. DR PDBsum; 1RBA; -. DR PDBsum; 1RUS; -. DR PDBsum; 2RUS; -. DR PDBsum; 5HQM; -. DR PDBsum; 5RUB; -. DR PDBsum; 9RUB; -. DR AlphaFoldDB; P04718; -. DR SMR; P04718; -. DR IntAct; P04718; 1. DR MINT; P04718; -. DR BioCyc; MetaCyc:MONOMER-13280; -. DR BRENDA; 4.1.1.39; 5420. DR SABIO-RK; P04718; -. DR EvolutionaryTrace; P04718; -. 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; IDA:CACAO. 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; 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 1: Evidence at protein level; KW 3D-structure; Calvin cycle; Carbon dioxide fixation; KW Direct protein sequencing; Lyase; Magnesium; Metal-binding; Monooxygenase; KW Oxidoreductase; Photosynthesis. FT CHAIN 1..466 FT /note="Ribulose bisphosphate carboxylase" FT /id="PRO_0000062666" FT ACT_SITE 166 FT /note="Proton acceptor" FT ACT_SITE 287 FT /note="Proton acceptor" FT BINDING 111 FT /ligand="substrate" FT /note="in homodimeric partner" FT BINDING 168 FT /ligand="substrate" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4" FT BINDING 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4" FT BINDING 288 FT /ligand="substrate" FT BINDING 321 FT /ligand="substrate" FT BINDING 368 FT /ligand="substrate" FT SITE 329 FT /note="Transition state stabilizer" FT MOD_RES 191 FT /note="N6-carboxylysine" FT /evidence="ECO:0000269|PubMed:1899197" FT MUTAGEN 193 FT /note="D->N: Loss of activity, decreased affinity for FT Mg(2+)." FT /evidence="ECO:0000269|PubMed:1606957, ECO:0000305" FT TURN 4..6 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 14..20 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 23..32 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:2RUS" FT HELIX 38..48 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:2RUS" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:1RBA" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 76..79 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 80..86 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 101..109 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 116..127 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 130..133 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 143..150 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 173..183 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:1RBA" FT HELIX 204..222 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 237..251 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 252..257 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 258..263 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 269..278 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 305..315 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 336..344 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 364..369 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 373..375 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 376..383 FT /evidence="ECO:0007829|PDB:5RUB" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:5RUB" FT TURN 394..397 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 403..419 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 423..428 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 431..439 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 441..447 FT /evidence="ECO:0007829|PDB:5RUB" FT HELIX 451..455 FT /evidence="ECO:0007829|PDB:5RUB" SQ SEQUENCE 466 AA; 50504 MW; 37D8C0076CAF7D54 CRC64; MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS TGTNVEVCTT DDFTRGVDAL VYEVDEAREL TKIAYPVALF HRNITDGKAM IASFLTLTMG NNQGMGDVEY AKMHDFYVPE AYRALFDGPS VNISALWKVL GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC HAFWLGGDFI KNDEPQGNQP FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI IARGEYVLET FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG PFYRQSWGGM KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI DGPVAGARSL RQAWQAWRDG VPVLDYAREH KELARAFESF PGDADQIYPG WRKALGVEDT RSALPA //