ID   I3Y992_THIV6            Unreviewed;       118 AA.
AC   I3Y992;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   02-SEP-2026, entry version 40.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE            Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
GN   Name=cbbS {ECO:0000256|HAMAP-Rule:MF_00859};
GN   OrderedLocusNames=Thivi_1571 {ECO:0000313|EMBL:AFL73560.1};
OS   Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS   violascens).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Chromatiales; Chromatiaceae; Thiocystis.
OX   NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL73560.1, ECO:0000313|Proteomes:UP000006062};
RN   [1] {ECO:0000313|EMBL:AFL73560.1, ECO:0000313|Proteomes:UP000006062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17096 / DSM 198 / 6111
RC   {ECO:0000313|Proteomes:UP000006062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of Thiocystis violascens DSM 198.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00859}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00859}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
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DR   EMBL; CP003154; AFL73560.1; -; Genomic_DNA.
DR   RefSeq; WP_014778026.1; NC_018012.1.
DR   AlphaFoldDB; I3Y992; -.
DR   STRING; 765911.Thivi_1571; -.
DR   KEGG; tvi:Thivi_1571; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_6; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000006062; Chromosome.
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   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00859}; Lyase {ECO:0000313|EMBL:AFL73560.1};
KW   Photorespiration {ECO:0000256|HAMAP-Rule:MF_00859};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00859};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006062}.
FT   DOMAIN          18..115
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   118 AA;  13672 MW;  282B1B0E9AA48DF0 CRC64;
     MSEMQDYPSS LEDVNSRKFE TFSYLPAMEA DKIRKQVEYI VAKGWNPAVE HTEPENAFDH
     YWYMWKLPMF GETNVDTILA EAEACHKAHP NNHVRLIGFD NYAQSKGAEM VVFRGKPV
//