RBL1B_ALLVD
ID RBL1B_ALLVD Reviewed; 471 AA.
AC P22859; D3RQ48;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:2211708};
GN Name=cbbL2 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338,
GN ECO:0000303|PubMed:1899846}; OrderedLocusNames=Alvin_2750;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=1899846; DOI=10.1016/0378-1119(91)90009-z;
RA Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K.,
RA Kobayashi K., Sugiura M.;
RT "Sequence and expression of genes encoding the large and small subunits of
RT ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum.";
RL Gene 97:55-62(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [3]
RP PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=2211708; DOI=10.1016/s0021-9258(17)44764-8;
RA Viale A.M., Kobayashi H., Akazawa T.;
RT "Distinct properties of Escherichia coli products of plant-type ribulose-
RT 1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from
RT the photosynthetic bacterium Chromatium vinosum.";
RL J. Biol. Chem. 265:18386-18392(1990).
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, ECO:0000269|PubMed:2211708};
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=32.8 uM for CO2 purified from A.vinosum in vivo
CC {ECO:0000269|PubMed:2211708};
CC KM=71.6 uM for CO2, enzyme expressed in E.coli
CC {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708};
CC KM=14.2 uM for D-ribulose 1,5-bisphosphate purified from A.vinosum in
CC vivo {ECO:0000269|PubMed:2211708};
CC KM=22.1 uM for D-ribulose 1,5-bisphosphate, enzyme expressed in
CC E.coli {ECO:0000269|PubMed:2211708};
CC Vmax=6.2 umol/min/mg enzyme purified from A.vinosum in vivo
CC {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708};
CC Vmax=5.9 umol/min/mg enzyme expressed in E.coli
CC {ECO:0000269|PubMed:2211708};
CC Note=This enzyme requires a lac or tac promoter for expression in
CC E.coli and has different kinetics than the enzyme purified in vivo,
CC suggesting this is not expressed in A.vinosum.
CC {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers. {ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000305|PubMed:1899846, ECO:0000305|PubMed:2211708}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {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}.
CC -!- CAUTION: In C.vinosum two similar set of genes code for RuBisCO large
CC and small chains: the RbcL-RbcS (this entry) and the RbcA-RbcB pair.
CC Under standard photoautotrophic culture conditions only the latter pair
CC seems active, the former probably being cryptic.
CC {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708}.
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DR EMBL; D90204; BAA14229.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63659.1; -; Genomic_DNA.
DR PIR; JQ0586; RKKRL2.
DR RefSeq; WP_012971927.1; NC_013851.1.
DR AlphaFoldDB; P22859; -.
DR SMR; P22859; -.
DR STRING; 572477.Alvin_2750; -.
DR EnsemblBacteria; ADC63659; ADC63659; Alvin_2750.
DR KEGG; alv:Alvin_2750; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_6; -.
DR OMA; GGGTQGH; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000001441; Chromosome.
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;
KW Disulfide bond; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW Oxidoreductase; Photosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2211708"
FT CHAIN 2..471
FT /note="Ribulose bisphosphate carboxylase large chain 2"
FT /id="PRO_0000062622"
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 DISULFID 240
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 145
FT /note="P -> R (in Ref. 1; BAA14229)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="Q -> R (in Ref. 1; BAA14229)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="N -> H (in Ref. 1; BAA14229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52284 MW; 08A26940B6458D97 CRC64;
MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV AAESSTGTWT
TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL FEEGSIVNVL TSLVGNVFGF
KAVRALRLED IRFPLHYVKT CGGPPNGIQV ERDRMDKYGR PFLGATVKPK LGLSAKNYGR
AVYEMLRGGL DFTKDDENVN SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC
EEMFKRAEFA KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED RSRGLFFDQD
WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ GHPWGNAAGA AANRVATEAC
VKARNEGVEI EKHAREVLSD AARHSPELAV AMETWKEIKF EFDVVDKLDA A
