RBS2_PETHY
ID RBS2_PETHY Reviewed; 180 AA.
AC P04715;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE AltName: Full=Ribulose bisphosphate carboxylase small chain SSU11A, chloroplastic;
DE Short=RuBisCO small subunit SSU11A;
DE Flags: Precursor;
GN Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Mitchell;
RX PubMed=3010233; DOI=10.1093/nar/14.8.3325;
RA Tumer N.E., Clark W.G., Tabor G.J., Hironaka C.M., Fraley R.T., Shah D.M.;
RT "The genes encoding the small subunit of ribulose-1,5-bisphosphate
RT carboxylase are expressed differentially in petunia leaves.";
RL Nucleic Acids Res. 14:3325-3342(1986).
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; X03821; CAA27445.1; -; Genomic_DNA.
DR AlphaFoldDB; P04715; -.
DR SMR; P04715; -.
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 3: Inferred from homology;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW Photosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 57..180
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031544"
SQ SEQUENCE 180 AA; 20335 MW; 4949933CA082FB54 CRC64;
MASSVMSSAA VATSTNAAQA SMVAPFTGLK SAASFPVSRK QNLDITSIAS NGGRVQCMQV
WPPYGKKKYE TLSYLPDLTD EQLLKEIEYL LNKGWVPCLE FETEHGFVYR EYHASPRYYD
GRYWTMWKLP MFGCTDATQV LGELQEAKKA YPNAWIRIIG FDNVRQVQCI SFIAYKPPGY
