ID A0A1M4XAB0_9ACTN Unreviewed; 110 AA.
AC A0A1M4XAB0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=SAMN02745225_01951 {ECO:0000313|EMBL:SHE90363.1};
OS Ferrithrix thermotolerans DSM 19514.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrithrix.
OX NCBI_TaxID=1121881 {ECO:0000313|EMBL:SHE90363.1, ECO:0000313|Proteomes:UP000184295};
RN [1] {ECO:0000313|Proteomes:UP000184295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19514 {ECO:0000313|Proteomes:UP000184295};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQUL01000036; SHE90363.1; -; Genomic_DNA.
DR RefSeq; WP_072791881.1; NZ_FQUL01000036.1.
DR AlphaFoldDB; A0A1M4XAB0; -.
DR STRING; 1121881.SAMN02745225_01951; -.
DR GeneID; 78386599; -.
DR OrthoDB; 25430at2; -.
DR Proteomes; UP000184295; 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:UP000184295}.
FT DOMAIN 12..109
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
SQ SEQUENCE 110 AA; 12882 MW; 5AFD45B637B19169 CRC64;
MAELQDYNST PKYETFSYLP AMTPEQVRKQ IVYLISQGWN PAIEHVEPEN ASRYFWYMWK
LPMFGEQSPD VVISELEACH RAHPGHHVRL IGYDNFSQSQ GIAFVVYRGR
//
