RBS_HELAN
ID RBS_HELAN Reviewed; 178 AA.
AC P08705;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3822825; DOI=10.1093/nar/15.3.1328;
RA Waksman G., Freyssinet G.;
RT "Nucleotide sequence of a cDNA encoding the ribulose-1,5-bisphosphate
RT carboxylase/oxygenase from sunflower (Helianthus annuus).";
RL Nucleic Acids Res. 15:1328-1328(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T 76 A;
RX PubMed=3658679; DOI=10.1093/nar/15.17.7181;
RA Waksman G., Lebrun M., Freyssinet G.;
RT "Nucleotide sequence of a gene encoding sunflower ribulose-1,5-bisphosphate
RT carboxylase/oxygenase small subunit (rbcs).";
RL Nucleic Acids Res. 15:7181-7181(1987).
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; X05079; CAA28737.1; -; mRNA.
DR EMBL; Y00431; CAA68490.1; -; Genomic_DNA.
DR PIR; A26852; RKFSS.
DR AlphaFoldDB; P08705; -.
DR SMR; P08705; -.
DR PRIDE; P08705; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr11g0470681; mRNA:HanXRQr2_Chr11g0470681; HanXRQr2_Chr11g0470681.
DR EnsemblPlants; mRNA:HanXRQr2_Chr11g0470711; mRNA:HanXRQr2_Chr11g0470711; HanXRQr2_Chr11g0470711.
DR Gramene; mRNA:HanXRQr2_Chr11g0470681; mRNA:HanXRQr2_Chr11g0470681; HanXRQr2_Chr11g0470681.
DR Gramene; mRNA:HanXRQr2_Chr11g0470711; mRNA:HanXRQr2_Chr11g0470711; HanXRQr2_Chr11g0470711.
DR OMA; WNPAIEH; -.
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..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 55..178
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031507"
SQ SEQUENCE 178 AA; 20211 MW; A9D1AAA930D4586D CRC64;
MASISSSVAT VSRTAPAQAN MVAPFTGLKS NAAFPTTKKA NDFSTLPSNG GRVQCMKVWP
PLGLKKYETL SYLPPLTETQ LAKEVDYLLR KKWVPCLEFE LEHGFVYREN ARSPGYYDGR
YWTMWKLPMF GCTDSAQVMK ELAECKKEYP QAWIRIIGFD NVRQVQCIMF IASRPDGY
