RBS2_PEA
ID RBS2_PEA Reviewed; 180 AA.
AC P00869;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PSS15;
DE AltName: Full=Ribulose bisphosphate carboxylase small chain 3C, chloroplastic;
DE Short=RuBisCO small subunit 3C;
DE Flags: Precursor;
GN Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-3C;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PSS15).
RC STRAIN=cv. Progress No. 9;
RX PubMed=6479146; DOI=10.1002/j.1460-2075.1984.tb02031.x;
RA Coruzzi G., Broglie R., Edwards C., Chua N.-H.;
RT "Tissue-specific and light-regulated expression of a pea nuclear gene
RT encoding the small subunit of ribulose-1,5-bisphosphate carboxylase.";
RL EMBO J. 3:1671-1679(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE (RBCS-3C).
RX PubMed=16453702; DOI=10.1002/j.1460-2075.1986.tb04467.x;
RA Fluhr R., Moses P., Morelli G., Coruzzi G., Chua N.-H.;
RT "Expression dynamics of the pea rbcS multigene family and organ
RT distribution of the transcripts.";
RL EMBO J. 5:2063-2071(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-180.
RX PubMed=6296093; DOI=10.1016/s0021-9258(18)32995-8;
RA Coruzzi G., Broglie R., Cashmore A., Chua N.-H.;
RT "Nucleotide sequences of two pea cDNA clones encoding the small subunit of
RT ribulose 1,5-bisphosphate carboxylase and the major chlorophyll a/b-binding
RT thylakoid polypeptide.";
RL J. Biol. Chem. 258:1399-1402(1983).
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; J01257; AAA33686.1; -; mRNA.
DR EMBL; X00806; CAA25390.1; -; Genomic_DNA.
DR EMBL; X04334; CAA27865.1; -; Genomic_DNA.
DR PIR; A01088; RKPMS5.
DR AlphaFoldDB; P00869; -.
DR SMR; P00869; -.
DR EnsemblPlants; Psat3g205240.1; Psat3g205240.1.cds; Psat3g205240.
DR Gramene; Psat3g205240.1; Psat3g205240.1.cds; Psat3g205240.
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..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_0000031541"
FT CONFLICT 25
FT /note="A -> G (in Ref. 3; AAA33686)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> F (in Ref. 3; AAA33686)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="G -> R (in Ref. 3; AAA33686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20244 MW; 212653E76E55205C CRC64;
MASMISSSAV TTVSRASRGQ SAAVAPFGGL KSMTGFPVKK VNTDITSITS NGGRVKCMQV
WPPIGKKKFE TLSYLPPLTR DQLLKEVEYL LRKGWVPCLE FELEKGFVYR EHNKSPGYYD
GRYWTMWKLP MFGTTDASQV LKELDEVVAA YPQAFVRIIG FDNVRQVQCI SFIAHTPESY
