RBL2_RHORU
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 03-AUG-2022, entry version 136.
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; Proteobacteria; 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}.
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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:MON-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; -; 1.
DR Gene3D; 3.30.70.150; -; 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; 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 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
