ID   RBS1_FRIAG              Reviewed;         179 AA.
AC   O24634;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 1/4 {ECO:0000305};
DE            Short=RuBisCO small subunit 1/4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=RBCS1;
GN   and
GN   Name=RBCS4;
OS   Fritillaria agrestis (Stinkbells).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Fritillaria.
OX   NCBI_TaxID=64177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Panico E., Baysdorfer C.;
RL   Submitted (SEP-1997) 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: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}.
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DR   EMBL; AF031543; AAB86853.1; -; mRNA.
DR   EMBL; AF024572; AAB84179.1; -; mRNA.
DR   AlphaFoldDB; O24634; -.
DR   SMR; O24634; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; -; 1.
DR   HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR   InterPro; IPR024681; RuBisCO_ssu.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; PTHR31262; 1.
DR   Pfam; PF12338; RbcS; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   PRINTS; PR00152; RUBISCOSMALL.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   2: Evidence at transcript level;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW   Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           59..179
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 1/4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031500"
SQ   SEQUENCE   179 AA;  19620 MW;  1695775BD611A765 CRC64;
     MAASSTMLSS VATAACAAPA QASMVAPFVG LKSTSAFPVT QKPATGLSTL PSNGGRVQCM
     KVWPIVGLKK FETLSYLPTL SVESLLKQIE YLIRNGWVPC LEFSLEGFVS RDNNKSPGYY
     DGRYWTMWKL PMFGCTDAAQ VVKEAAECKK EYPAAFIRVI GFDNVRQVQC VSFIVERPE