RBL1A_ALLVD
ID RBL1A_ALLVD Reviewed; 472 AA.
AC P22849; D3RSZ1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 4.
DT 03-AUG-2022, entry version 111.
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, ECO:0000269|PubMed:3579306};
GN Name=cbbL1 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=rbcA {ECO:0000303|PubMed:2708310}; OrderedLocusNames=Alvin_1365;
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], PROTEIN SEQUENCE OF 3-9, AND INDUCTION.
RX PubMed=2708310; DOI=10.1128/jb.171.5.2391-2400.1989;
RA Viale A.M., Kobayashi H., Akazawa T.;
RT "Expressed genes for plant-type ribulose 1,5-bisphosphate
RT carboxylase/oxygenase in the photosynthetic bacterium Chromatium vinosum,
RT which possesses two complete sets of the genes.";
RL J. Bacteriol. 171:2391-2400(1989).
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 2-25, 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).
RN [4]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=Strain D;
RX PubMed=3579306; DOI=10.1016/0003-9861(87)90081-6;
RA Torres-Ruiz J., McFadden B.A.;
RT "The nature of L8 and L8S8 forms of ribulose bisphosphate
RT carboxylase/oxygenase from Chromatium vinosum.";
RL Arch. Biochem. Biophys. 254:63-68(1987).
RN [5]
RP PROTEIN SEQUENCE OF 2-37.
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).
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:3579306};
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:3579306};
CC KM=32.5 uM for CO2, enzyme expressed in E.coli
CC {ECO:0000269|PubMed:3579306};
CC KM=14.2 uM for D-ribulose 1,5-bisphosphate purified from A.vinosum in
CC vivo {ECO:0000269|PubMed:3579306};
CC KM=14.0 uM for D-ribulose 1,5-bisphosphate, enzyme expressed in
CC E.coli {ECO:0000269|PubMed:3579306};
CC Vmax=6.2 umol/min/mg enzyme purified from A.vinosum in vivo
CC {ECO:0000269|PubMed:3579306};
CC Vmax=6.4 umol/min/mg enzyme expressed in E.coli
CC {ECO:0000269|PubMed:3579306};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:2211708,
CC ECO:0000305|PubMed:3579306}.
CC -!- INDUCTION: Expressed when grown photoautotrophically (at protein
CC level). {ECO:0000269|PubMed:2708310, ECO:0000269|PubMed:3579306}.
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 and the RbcA-RbcB pair (this entry).
CC Under standard photoautotrophic culture conditions only the latter pair
CC seems active, the former probably being cryptic.
CC {ECO:0000269|PubMed:2211708, ECO:0000269|PubMed:2708310,
CC ECO:0000269|PubMed:3579306}.
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DR EMBL; M26396; AAA23328.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC62300.1; -; Genomic_DNA.
DR PIR; A32303; RKKRL1.
DR RefSeq; WP_012970574.1; NC_013851.1.
DR AlphaFoldDB; P22849; -.
DR SMR; P22849; -.
DR STRING; 572477.Alvin_1365; -.
DR EnsemblBacteria; ADC62300; ADC62300; Alvin_1365.
DR KEGG; alv:Alvin_1365; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_6; -.
DR OMA; EYRETYW; -.
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; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1899846,
FT ECO:0000269|PubMed:2211708, ECO:0000269|PubMed:3579306"
FT CHAIN 2..472
FT /note="Ribulose bisphosphate carboxylase large chain 1"
FT /id="PRO_0000062621"
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 2
FT /note="A -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3579306"
FT CONFLICT 17
FT /note="W -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3579306"
FT CONFLICT 146
FT /note="G -> A (in Ref. 1; AAA23328)"
SQ SEQUENCE 472 AA; 52510 MW; 6B7544F239AE5F8A CRC64;
MAKTYSAGVK EYRETYWMPN YTPKDTDILA CFKITPQAGV PREEAAAAVA AESSTGTWTT
VWTDLLTDLD YYKGRAYAIE DVPGDDTCFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK
AVRALRLEDV RFPIAYVMTC NGPPHGIQVE RDIMNKYGRP MLGCTIKPKL GLSAKNYGRA
VYECLRGGLD FTKDDENVNS QPFMRWRQRF DFVMDAIDKA ERETGERKGH YLNVTAPTPE
EMYKRAEYAK EIGAPIIMHD YITGGFCANT GLAQWCRDNG VLLHIHRAMH AVLDRNPHHG
IHFRVLTKIL RLSGGDHLHT GTVVGKLEGD RASTLGWIDL LRESYIKEDR SRGLFFDQDW
GSMPGAFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTLG HPWGNAAGAC ANRVALEACV
EARNQGVAIE KEGKDVLTKA AASSPELKIA METWKEIKFE FDTVDKLDIA HK
