RBL1A_HYDMR
ID RBL1A_HYDMR Reviewed; 472 AA.
AC Q59458; Q75W45;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain 1 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Name=cbbL1 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=cbbL-1 {ECO:0000303|PubMed:9531639};
OS Hydrogenovibrio marinus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=28885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EXPRESSION IN E.COLI.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX PubMed=9531639; DOI=10.1007/s002030050584;
RA Nishihara H., Yaguchi T., Chung S.-Y., Suzuki K., Yanagi M., Yamasato K.,
RA Kodama T., Igarashi Y.;
RT "Phylogenetic position of an obligately chemoautotrophic, marine hydrogen-
RT oxidizing bacterium, Hydrogenovibrio marinus, on the basis of 16S rRNA gene
RT sequences and two form I RuBisCO gene sequences.";
RL Arch. Microbiol. 169:364-368(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION OF EXPRESSION BY CO(2) IN
RP H.MARINUS.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX PubMed=15317772; DOI=10.1128/jb.186.17.5685-5691.2004;
RA Yoshizawa Y., Toyoda K., Arai H., Ishii M., Igarashi Y.;
RT "CO2-responsive expression and gene organization of three ribulose-1,5-
RT bisphosphate carboxylase/oxygenase enzymes and carboxysomes in
RT Hydrogenovibrio marinus strain MH-110.";
RL J. Bacteriol. 186:5685-5691(2004).
RN [3]
RP CHARACTERIZATION IN E.COLI, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX DOI=10.1016/S0922-338X(97)86759-1;
RA Hayashi N.R., Oguni A., Yaguchi T., Chung S.-Y., Nishihara H., Kodama T.,
RA Igarashi Y.;
RT "Different properties of gene products of three sets ribulose 1,5-
RT bisphosphate carboxylase/oxygenase from a marine obligately autotrophic
RT hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110.";
RL J. Ferment. Bioeng. 85:150-155(1998).
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:0000269|Ref.3}.
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|Ref.3};
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|Ref.3};
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 Vmax=1.2 umol/min/mg enzyme with CO(2) as substrate, expressed in
CC E.coli {ECO:0000269|Ref.3};
CC Note=The CO(2)/O(2) specificity factor (tau) is 26.6.
CC {ECO:0000269|Ref.3};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000269|Ref.3, ECO:0000305}.
CC -!- INDUCTION: Both mRNA and protein accumulate at 2% and 0.03% CO(2), but
CC not at 15% or 0.15% CO(2) (at protein level).
CC {ECO:0000269|PubMed:15317772}.
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,
CC ECO:0000305|PubMed:9531639}.
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DR EMBL; D43621; BAA07729.1; -; Genomic_DNA.
DR EMBL; AB122069; BAD15307.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59458; -.
DR SMR; Q59458; -.
DR STRING; 28885.EI16_08840; -.
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; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1..472
FT /note="Ribulose bisphosphate carboxylase large chain 1"
FT /id="PRO_0000062624"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 115
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 193
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 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 326
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 193
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 298
FT /note="L -> M (in Ref. 2; BAD15307)"
FT /evidence="ECO:0000305"
FT CONFLICT 332..334
FT /note="GSD -> EAT (in Ref. 2; BAD15307)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="I -> L (in Ref. 2; BAD15307)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="V -> A (in Ref. 2; BAD15307)"
FT /evidence="ECO:0000305"
FT CONFLICT 411..413
FT /note="VNL -> ANR (in Ref. 2; BAD15307)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..441
FT /note="DG -> AA (in Ref. 2; BAD15307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52488 MW; 71FCAE86F7CF2530 CRC64;
MAKTYNAGVK EYRETYWMPE YEPKDSDFLA CFKVVPQPGV PREEIAAAVA AESSTGTWTT
VWTDLLTDLD YYKGRAYRIE DVPGDDSAFY AFIAYPIDLF EEGSIVSVMT SLVGNVFGFK
ALRSIRLEDI RFPLAYVMTC GGPPHGIQVE RDKMDKYGRP MLGCTIKPKL GLSAKNYGRA
VYECLRGGLD FTKDDENVTS QPFMRWRDRF LFCQDAIEKA QDETGERTGH YLNATAGTPE
EMYERAEFAK EIGSPIVMHD FLTGGLTANT GLANYCRKNG LLLHIHRAMH GVIDRNPLHG
IHFRVLSKVL RLSGGDHLHS GTVVGKLEGD RGSDLGWIDI MRDSFIAEDR SRGIMFDQDF
GEMPGVIPVA SGGIHVWHMP ALVAIFGDDS VLQFGGGTIG HPWGNAVGAA VNLVALEACV
QARNEGQEIE KNGKEILTND GKHSPELKIA METWKEIKFE FDTVDKLDLS HK
