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Database: UniProt
Entry: A0A1Y6CV65_9GAMM
LinkDB: A0A1Y6CV65_9GAMM
Original site: A0A1Y6CV65_9GAMM 
ID   A0A1Y6CV65_9GAMM        Unreviewed;       114 AA.
AC   A0A1Y6CV65;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
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   ORFNames=SAMN02949497_1867 {ECO:0000313|EMBL:SMF94549.1};
OS   Methylomagnum ishizawai.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomagnum.
OX   NCBI_TaxID=1760988 {ECO:0000313|EMBL:SMF94549.1, ECO:0000313|Proteomes:UP000192923};
RN   [1] {ECO:0000313|EMBL:SMF94549.1, ECO:0000313|Proteomes:UP000192923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=175 {ECO:0000313|EMBL:SMF94549.1,
RC   ECO:0000313|Proteomes:UP000192923};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; FXAM01000001; SMF94549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6CV65; -.
DR   STRING; 1760988.SAMN02949497_1867; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000192923; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000192923}.
FT   DOMAIN          13..110
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   114 AA;  13192 MW;  DDBCA4BC56050583 CRC64;
     MSEIRDFSPS SRKLGTFSYL KEMEPERIRK QVEYIVRRGW NPAVEHSEPE NAFDHYWYMW
     KLPLFGETDV DKILAEAAAC RAAHPHNHVR LVGYDTRRQS QGAALVVYRG LAAA
//
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