RBS1_ACIFR
ID RBS1_ACIFR Reviewed; 110 AA.
AC P28896;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 91.
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}; Synonyms=rbcS1;
OS Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=920;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1718945; DOI=10.1128/jb.173.22.7313-7323.1991;
RA Kusano T., Takeshima T., Inoue C., Sugawara K.;
RT "Evidence for two sets of structural genes coding for ribulose bisphosphate
RT carboxylase in Thiobacillus ferrooxidans.";
RL J. Bacteriol. 173:7313-7323(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 -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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 A.ferrooxidans two similar set of genes code for RuBisCO
CC large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets.
CC {ECO:0000305}.
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DR EMBL; D90113; BAA14142.1; -; Genomic_DNA.
DR PIR; B41323; B41323.
DR AlphaFoldDB; P28896; -.
DR SMR; P28896; -.
DR STRING; 380394.Lferr_1388; -.
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 3: Inferred from homology;
KW Calvin cycle; Carbon dioxide fixation.
FT CHAIN 1..110
FT /note="Ribulose bisphosphate carboxylase small subunit 1"
FT /id="PRO_0000198629"
SQ SEQUENCE 110 AA; 12880 MW; 0078A2F3248AD5D8 CRC64;
MADIQDYNST PKYETFSYLP AMGPEKMRRQ IAYLINQGWN PGIEHVEPER ASTYYWYMWK
LPMFGEQSVD TVIMELEACH RAHPGHHVRL VGYDNYSQSQ GSAFVVFRGR