ID   RBS_MANES               Reviewed;         182 AA.
AC   Q42915;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00860};
DE   Flags: Precursor;
GN   Name=RBCS {ECO:0000255|HAMAP-Rule:MF_00860};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7626783; DOI=10.3109/10425179509030971;
RA   Mak Y.M., Ho K.K.;
RT   "Sequence of cassava ribulose-1,5-bisphosphate carboxylase small subunit
RT   precursor cDNA.";
RL   DNA Seq. 5:229-232(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Brazil;
RX   PubMed=10647822; DOI=10.3109/10425179909033946;
RA   Yeo T.W., Mak Y.M., Ho K.K.;
RT   "Rubisco small subunit gene family in Cassava.";
RL   DNA Seq. 10:189-194(1999).
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; M96583; AAA99429.1; -; mRNA.
DR   EMBL; AF101231; AAF06099.1; -; mRNA.
DR   AlphaFoldDB; Q42915; -.
DR   SMR; Q42915; -.
DR   STRING; 3983.cassava4.1_017243m; -.
DR   PRIDE; Q42915; -.
DR   EnsemblPlants; OAY50455; OAY50455; MANES_05G137400.
DR   Gramene; OAY50455; OAY50455; MANES_05G137400.
DR   OMA; GRCWIMW; -.
DR   OrthoDB; 1258997at2759; -.
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..182
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031524"
SQ   SEQUENCE   182 AA;  20411 MW;  F8EFBFD62C69516D CRC64;
     MASSMLSTAT VASINRVSPA QATMVAPFTG LKSTPVFPTT RKTNSDITSI TSNGGKVQCM
     KVWPTLGMKK FETLSYLPPL TREQLASEVE YLLRSGWIPC LEFELEHGLV YREHARVPGY
     YDGRYWTMWK LPMFGCTDAA QVLKELDELI KHHPDGYARI IGFDNVRQVQ CISFLAYKPP
     GA