RBS_BETPN
ID RBS_BETPN Reviewed; 182 AA.
AC Q96542;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 88.
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}; Synonyms=RBCS1;
OS Betula pendula (European white birch) (Betula verrucosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Betula.
OX NCBI_TaxID=3505;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Valjakka M., Vapaavuori E., Haeggman H., Kangasjaervi J.;
RT "A cDNA from Silver Birch (Betula pendula Roth) encoding the small subunit
RT of ribulose-1,5-bisphosphate carboxylase/oxygenase.";
RL (er) Plant Gene Register PGR97-100(1997).
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; Y07779; CAA69102.1; -; mRNA.
DR AlphaFoldDB; Q96542; -.
DR SMR; Q96542; -.
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_0000031468"
SQ SEQUENCE 182 AA; 20448 MW; 93D9177D23475DFC CRC64;
MACSMISSAT VAAVSRASPA QSSMVAPFTC LKSTSAFPVT QKTNNDITSI ASNGGRVQCM
QVWPPLGLKK FETLSYLPPL SSEQLAKEVD YLLRKNLIPC LEFELEHGFV YREHNRSPGY
YDGRYWTMWK LPMFGCNDSS QVLKELEECK KAYPSAFIRI IGFDNKRQVQ IISFIAYKPP
GV