RBS1_ALLVD
ID RBS1_ALLVD Reviewed; 118 AA.
AC P22850; D3RSZ2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 5.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00859};
DE Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00859};
GN Name=cbbS1 {ECO:0000255|HAMAP-Rule:MF_00859};
GN Synonyms=rbcB {ECO:0000303|PubMed:2708310}; OrderedLocusNames=Alvin_1366;
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 2-8, AND INDUCTION.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
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 2-50, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP 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 [4]
RP PROTEIN SEQUENCE OF 2-27, FUNCTION, SUBUNIT, AND INDUCTION.
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 [5]
RP PROTEIN SEQUENCE OF 2-30.
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. Although the small subunit is not catalytic it is
CC essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00859,
CC ECO:0000305|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: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 and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00859, 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_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 and the RbcA-RbcB pair (this entry).
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,
CC ECO:0000269|PubMed:2708310}.
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DR EMBL; M26396; AAA23329.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC62301.1; -; Genomic_DNA.
DR PIR; B32303; RKKRS1.
DR RefSeq; WP_012970575.1; NC_013851.1.
DR AlphaFoldDB; P22850; -.
DR SMR; P22850; -.
DR STRING; 572477.Alvin_1366; -.
DR EnsemblBacteria; ADC62301; ADC62301; Alvin_1366.
DR KEGG; alv:Alvin_1366; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_6; -.
DR OMA; WNPAIEH; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1899846,
FT ECO:0000269|PubMed:2211708, ECO:0000269|PubMed:2708310,
FT ECO:0000269|PubMed:3579306"
FT CHAIN 2..118
FT /note="Ribulose bisphosphate carboxylase small subunit 1"
FT /id="PRO_0000198612"
FT CONFLICT 5
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3579306"
FT CONFLICT 10
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3579306"
FT CONFLICT 27
FT /note="A -> R (in Ref. 1; AAA23329)"
FT CONFLICT 30..31
FT /note="AD -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3579306"
FT CONFLICT 40
FT /note="I -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3579306"
SQ SEQUENCE 118 AA; 13794 MW; 43B8ADB8ECD7FABE CRC64;
MSEMQDYSSS LEDVNSRKFE TFSYLPAMDA DRIRKQVEYI VSKGWNPAIE HTEPENAFDH
YWYMWKLPMF GETDIDTILK EAEACHKAHP NNHVRLIGFD NYAQSKGAEM VVYRGKPV
