RBS2_ALLVD
ID RBS2_ALLVD Reviewed; 113 AA.
AC P22860; D3RQ47;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00859};
DE Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00859};
GN Name=cbbS2 {ECO:0000255|HAMAP-Rule:MF_00859};
GN Synonyms=rbcS {ECO:0000303|PubMed:1899846}; OrderedLocusNames=Alvin_2749;
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, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 1-24, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 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. Although the small subunit is not catalytic it is
CC essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00859,
CC ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708}.
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 and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:2211708}.
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_00859}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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 being probably cryptic.
CC {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708}.
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DR EMBL; D90204; BAA14230.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63658.1; -; Genomic_DNA.
DR PIR; JQ0587; RKKRS2.
DR RefSeq; WP_012971926.1; NC_013851.1.
DR AlphaFoldDB; P22860; -.
DR SMR; P22860; -.
DR STRING; 572477.Alvin_2749; -.
DR EnsemblBacteria; ADC63658; ADC63658; Alvin_2749.
DR KEGG; alv:Alvin_2749; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_6; -.
DR OMA; VYIINQG; -.
DR OrthoDB; 1708389at2; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 1.
DR HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR InterPro; IPR024681; RuBisCO_ssu.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Direct protein sequencing;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..113
FT /note="Ribulose bisphosphate carboxylase small subunit 2"
FT /id="PRO_0000198613"
FT CONFLICT 109
FT /note="V -> A (in Ref. 1; BAA14230)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="A -> P (in Ref. 1; BAA14230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 113 AA; 13393 MW; 00376BC870FF3399 CRC64;
MNTASSMGDH ATIGRYETFS YLPPLNREEI LEQILYILDN GWNASLEHEH PDRAFEYYWP
MWKMPFFGEQ DPNVILTEIE SCRRSYPDHH VRLVGYDTYA QSKGHSFLVH RAR
