RBL_HYDTE
ID RBL_HYDTE Reviewed; 474 AA.
AC Q51856;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
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};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila).
OC Bacteria; Proteobacteria; Hydrogenophilalia; Hydrogenophilales;
OC Hydrogenophilaceae; Hydrogenophilus.
OX NCBI_TaxID=297;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TH-1 / NBRC 14978;
RX PubMed=7883189; DOI=10.1016/0378-1119(94)00808-6;
RA Yokoyama K., Hayashi N.R., Arai H., Chung S.Y., Igarashi Y., Kodama T.;
RT "Genes encoding RubisCO in Pseudomonas hydrogenothermophila are followed by
RT a novel cbbQ gene similar to nirQ of the denitrification gene cluster from
RT Pseudomonas species.";
RL Gene 153:75-79(1995).
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 -!- 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};
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 -!- 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 -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
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; D30764; BAA06437.1; -; Genomic_DNA.
DR AlphaFoldDB; Q51856; -.
DR SMR; Q51856; -.
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 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 3: Inferred from homology;
KW Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1..474
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062640"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 117
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 195
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 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 328
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 195
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ SEQUENCE 474 AA; 53286 MW; 7C54A07E0CDC032C CRC64;
MSQPKRYEAG VKEYRETYWE PTYVPKDSDF LAVFKIVPQP GVPREESAAA VAAESSTATW
TTVWTDLLTD LYYYKGRAYA IEDVPGDDEA FYAFIAYPMG LFEEGSVVNV FTSLVGNVFG
FKAVRSLRLE DVRIPLWFVT TCPGPPHGIY VERDKLNKYG RPLLGCTIKP KLGLSAKNYG
RAVYECLRGG LDFTKDDENV NSQPFMRWRD RFLFCQEAIE KAQAETGERK GHYMNVTGPT
MEEIYKRAEF AKEIGTPIIM IDYLTVGWAA TQSLSKWCRD NGMLLHVHRA MHAVIDRNPK
HGINFRVLAK IMRLIGGDHL HSGTVVGKLE GDRAATLGWI DLMRDRYVKA DRSRGIFFDQ
DWGQMPGMFP VASGGIHVWH MPALVSIFGD DSVLQFGGGT IGHPWGNAAG ACANRVALEA
CVKARNEGLP IEKMGREILT EAAKSCPELK VAMETWKEVK FDFDTVDKLD VQHR
