RBL_HYDPS
ID RBL_HYDPS Reviewed; 473 AA.
AC Q9ZB35;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 89.
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};
GN Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=47421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 1084 / Z-1107;
RX PubMed=9856338;
RA Lee S.N., Kim Y.M.;
RT "Cloning and characterization of ribulose bisphosphate carboxylase gene of
RT a carboxydobacterium, Hydrogenophagea pseudoflava DSM 1084.";
RL Mol. Cells 8:524-529(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND CHARACTERIZATION.
RC STRAIN=DSM 1084 / Z-1107;
RX PubMed=9264026;
RA Kim E.Y., Ro Y.T., Kim Y.M.;
RT "Purification and some properties of ribulose 1,5-bisphosphate
RT carboxylases/oxygenases from Acinetobacter sp. strain JC1 and
RT Hydrogenophaga pseudoflava.";
RL Mol. Cells 7:380-388(1997).
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; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for ribulose 1,5-bisphosphate;
CC KM=16.4 uM for CO(2);
CC Vmax=436.2 nmol/min/ug enzyme with ribulose 1,5-bisphosphate as
CC substrate;
CC Vmax=777.8 nmol/min/ug enzyme with CO(2) as substrate;
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000305|PubMed:9264026}.
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; U55037; AAD10331.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZB35; -.
DR SMR; Q9ZB35; -.
DR PRIDE; Q9ZB35; -.
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 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Direct protein sequencing; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9264026"
FT CHAIN 2..473
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062626"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 116
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 194
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 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 327
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 194
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 14
FT /note="R -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52692 MW; 87F82E96F8A35C59 CRC64;
MATKTYNAGV KEYRSTYWEP HYTPKDTDIL ACFKITPQPG VDREEVAAAV AAESSTGTWT
TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF
KALRALRSED VRFPIAYVKT CGGPPHGIQV ERDIMNKYGR PLLGCTIKPK LGLSGKNYGR
AVYECLRGGL DFTKDDENVN SQPFMRWPQR FDFEQEAIEK AHGETGERKV HYLNVTAPTP
GEMYKRAEYA KELGAPIIMH DYLTGGLCAN TGLANWCRDN GMLLHIHRAM HAELDRNPHH
GIHFRVLTKV LRLSGRDHLH SGTVVGKLEG DRASTLGWID IMRDTFIKED RSRGIFFDQD
FGSMPGVMPV ASGGIHVWHM PALVNIFGDD SVLQFGGGTV GHPWGNAPGA TANRVELEAC
VKARNEGIAV EKEGKAVLTE AANDSPELKI AMETWKEIKF EFDTVDKLDI AHK
