ID RBS3_ACEAT Reviewed; 182 AA.
AC P16136;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Flags: Precursor;
GN Name=RBCS3 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-3;
OS Acetabularia acetabulum (Mermaid's wine glass) (Acetabularia mediterranea).
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Dasycladales; Polyphysaceae; Acetabularia.
OX NCBI_TaxID=35845;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=17;
RX PubMed=2573818; DOI=10.1007/bf00332408;
RA Schneider S.U., Leible M.B., Yang X.P.;
RT "Strong homology between the small subunit of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase of two species of Acetabularia and the occurrence of
RT unusual codon usage.";
RL Mol. Gen. Genet. 218:445-452(1989).
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_00860}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_00860}.
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_00860}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51813; CAA36110.1; -; mRNA.
DR PIR; S07117; RKJK3M.
DR AlphaFoldDB; P16136; -.
DR SMR; P16136; -.
DR GO; GO:0009507; C:chloroplast; 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 PANTHER; PTHR31262:SF28; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 1; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE 2: Evidence at transcript level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW Photosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 42..182
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031456"
SQ SEQUENCE 182 AA; 20571 MW; 5D6D029A931C6476 CRC64;
MASIMMNKSV VLSKECAKPL ASPKVTLNKR GFATTIATKN RGMMVWQPFN NKMFETFSFL
PPLTDEQISK QVDYILINSW TPCLEFAASD QAYAGNENCI RMGPVASTYQ DNRYWTMWKL
PMFGCTDASQ VLSEIQACTK AFPDAYIRLV CFDANRQVQI SGFLVHRPPS ATDYKLPADR
QV
//
