RBL1_CERSP
ID RBL1_CERSP Reviewed; 486 AA.
AC P27997;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:9882445};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=cbbL1, rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=HR;
RX PubMed=1907281; DOI=10.1016/s0021-9258(18)98734-x;
RA Gibson J.L., Falcone D.L., Tabita F.R.;
RT "Nucleotide sequence, transcriptional analysis, and expression of genes
RT encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides.";
RL J. Biol. Chem. 266:14646-14653(1991).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LEU-341.
RC STRAIN=FI;
RX PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA Horken K.M., Tabita F.R.;
RT "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT molecules that possess different CO2/O2 substrate specificities.";
RL Arch. Biochem. Biophys. 361:183-194(1999).
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_01338,
CC ECO:0000269|PubMed:9882445}.
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_01338, ECO:0000269|PubMed:9882445};
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_01338,
CC ECO:0000269|PubMed:9882445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for ribulose 1,5-bisphosphate {ECO:0000269|PubMed:9882445};
CC KM=22 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate
CC {ECO:0000269|PubMed:9882445};
CC Note=The CO(2)/O(2) specificity factor (tau) is 56.;
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:9882445}.
CC -!- INDUCTION: Expression of this operon predominates when carbon dioxide
CC is limiting. {ECO:0000269|PubMed:1907281}.
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:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; M64624; AAA26115.1; -; Genomic_DNA.
DR PIR; D40767; RKRFAL.
DR RefSeq; WP_002721829.1; NZ_WTFI01000004.1.
DR PDB; 5NV3; EM; 3.39 A; A/B/C/D/E/F/G/H=13-479.
DR PDBsum; 5NV3; -.
DR AlphaFoldDB; P27997; -.
DR SMR; P27997; -.
DR GeneID; 57471612; -.
DR GeneID; 67448053; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR SABIO-RK; P27997; -.
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; -; 1.
DR Gene3D; 3.30.70.150; -; 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; 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; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis.
FT CHAIN 1..486
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062647"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 295
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 125
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 335
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 203
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MUTAGEN 341
FT /note="L->M: Increases KM for CO(2), decreases KM for
FT ribulose 1,5-bisphosphate."
FT /evidence="ECO:0000269|PubMed:9882445"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:5NV3"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 216..234
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:5NV3"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5NV3"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 415..434
FT /evidence="ECO:0007829|PDB:5NV3"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:5NV3"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:5NV3"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:5NV3"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5NV3"
SQ SEQUENCE 486 AA; 53686 MW; 82B91D700303C3C0 CRC64;
MDTKTTEIKG KERYKAGVLK YAQMGYWDGD YVPKDTDVLA LFRITPQEGV DPVEAAAAVA
GESSTATWTV VWTDRLTACD SYRAKAYRVE PVPGTPGQYF CYVAYDLILF EEGSIANLTA
SIIGNVFSFK PLKAARLEDM RFPVAYVKTY KGPPTGIVGE RERLDKFGKP LLGATTKPKL
GLSGKNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH
YLNITAGTME EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC REPFNTVDLP
RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLSLFGDDVV LQFGGGTIGH PMGIQAGATA
NRVALEAMVL ARNEGRNIDV EGPEILRAAA KWCKPLEAAL DTWGNITFNY TSTDTSDFVP
TASVAM
