RBL1C_CUPNE
ID RBL1C_CUPNE Reviewed; 486 AA.
AC P0C2C2; P09657; P77811;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain, chromosomal;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
GN Name=cbbL1; Synonyms=cbbL, cbxLC, cfxLC;
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBOXYLATION AT LYS-204.
RC STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R;
RX PubMed=2820933; DOI=10.1128/jb.169.10.4547-4558.1987;
RA Andersen K., Caton J.;
RT "Sequence analysis of the Alcaligenes eutrophus chromosomally encoded
RT ribulose bisphosphate carboxylase large and small subunit genes and their
RT gene products.";
RL J. Bacteriol. 169:4547-4558(1987).
RN [2]
RP SEQUENCE REVISION.
RA Andersen K.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-467 OF UNACTIVATED HOLOENYZYME,
RP AND SUBUNIT.
RC STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R;
RX PubMed=10329167; DOI=10.1006/jmbi.1999.2701;
RA Hansen S., Vollan V.B., Hough E., Andersen K.;
RT "The crystal structure of rubisco from Alcaligenes eutrophus reveals a
RT novel central eight-stranded beta-barrel formed by beta-strands from four
RT subunits.";
RL J. Mol. Biol. 288:609-621(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.
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 Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. A
CC disulfide link might be formed within the large subunit homodimers.
CC {ECO:0000269|PubMed:10329167}.
CC -!- PTM: A disulfide bond might be able to form between Cys-278 in the
CC large chain dimeric partners within the hexadecamer.
CC {ECO:0000305|PubMed:10329167}.
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 -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
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; M17744; AAC28129.1; -; Genomic_DNA.
DR PIR; A26954; RKALLE.
DR PDB; 1BXN; X-ray; 2.70 A; A/C/E/G=1-486.
DR PDBsum; 1BXN; -.
DR AlphaFoldDB; P0C2C2; -.
DR SMR; P0C2C2; -.
DR EvolutionaryTrace; P0C2C2; -.
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; Disulfide bond; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN 1..486
FT /note="Ribulose bisphosphate carboxylase large chain,
FT chromosomal"
FT /id="PRO_0000062641"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT BINDING 126
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT BINDING 176
FT /ligand="substrate"
FT BINDING 180
FT /ligand="substrate"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 297
FT /ligand="substrate"
FT BINDING 329
FT /ligand="substrate"
FT BINDING 381
FT /ligand="substrate"
FT SITE 336
FT /note="Transition state stabilizer"
FT MOD_RES 204
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:2820933"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1BXN"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 217..235
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:1BXN"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1BXN"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 341..352
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:1BXN"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 414..435
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 439..453
FT /evidence="ECO:0007829|PDB:1BXN"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:1BXN"
SQ SEQUENCE 486 AA; 53840 MW; 66EAB4A11982FAB5 CRC64;
MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG VDPVEAAAAV
AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT
ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK
LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG
SYLNVTAGTM EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTQTDL
TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT
ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCAPLRAA LDTWGDITFN YTPTDTSDFV
PTASVA
