ID Q3AWU2_SYNS9 Unreviewed; 113 AA.
AC Q3AWU2;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 Synonyms=rbcS {ECO:0000256|HAMAP-Rule:MF_00859};
GN OrderedLocusNames=Syncc9902_1613 {ECO:0000313|EMBL:ABB26571.1};
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB26571.1, ECO:0000313|Proteomes:UP000002712};
RN [1] {ECO:0000313|Proteomes:UP000002712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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 in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site. Although the
CC small subunit is not catalytic it is essential for maximal activity.
CC {ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {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; CP000097; ABB26571.1; -; Genomic_DNA.
DR RefSeq; WP_006853347.1; NC_007513.1.
DR AlphaFoldDB; Q3AWU2; -.
DR STRING; 316279.Syncc9902_1613; -.
DR KEGG; sye:Syncc9902_1613; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_3; -.
DR OrthoDB; 9788955at2; -.
DR Proteomes; UP000002712; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 Bacterial microcompartment {ECO:0000256|HAMAP-Rule:MF_00859};
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}; Carboxysome {ECO:0000256|HAMAP-Rule:MF_00859};
KW Lyase {ECO:0000313|EMBL:ABB26571.1};
KW Photorespiration {ECO:0000256|HAMAP-Rule:MF_00859};
KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00859}.
FT DOMAIN 15..112
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
SQ SEQUENCE 113 AA; 12929 MW; 9FF3414C776391F4 CRC64;
MPFQSTVGDY QTVATLETFG FLPPMTQDEI YDQIAYIIAQ GWSPLVEHVH PSNSMATYWS
YWKLPFFGEK DLNVVVSELE ACHRAYPDHH VRIVGYDAYT QGQGSCFVVF EGR
//
