ID   RBS3_PEA                Reviewed;         180 AA.
AC   P07689; P12467;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   AltName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 3A;
DE            Short=RuBisCO small subunit 3A;
DE   Flags: Precursor;
GN   Name=RBCS.3A;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
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].
RC   STRAIN=cv. Progress No. 9;
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3827863; DOI=10.1042/bj2400709;
RA   Anderson S., Smith S.M.;
RT   "Synthesis of the small subunit of ribulose-bisphosphate carboxylase from
RT   genes cloned into plasmids containing the SP6 promoter.";
RL   Biochem. J. 240:709-715(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-180.
RX   PubMed=3042319; DOI=10.1089/dna.1.1988.7.329;
RA   Hunt A.G.;
RT   "Identification and characterization of cryptic polyadenylation sites in
RT   the 3' region of a pea ribulose-1,5-bisphosphate carboxylase small subunit
RT   gene.";
RL   DNA 7:329-336(1988).
RN   [4] {ECO:0007744|PDB:4HHH}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 58-180 OF INACTIVE HOLOENZYME IN
RP   COMPLEX WITH RIBULOSE 1,5-BISPHOSPHATE, FUNCTION, AND SUBUNIT.
RX   PubMed=23295478; DOI=10.1107/s1744309112047549;
RA   Loewen P.C., Didychuk A.L., Switala J., Perez-Luque R., Fita I.,
RA   Loewen M.C.;
RT   "Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.";
RL   Acta Crystallogr. F 69:10-14(2013).
RN   [5] {ECO:0007744|PDB:4MKV}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 58-180 OF INACTIVE HOLOENZYME IN
RP   COMPLEX WITH RIBULOSE 1,5-BISPHOSPHATE, FUNCTION, AND SUBUNIT.
RX   PubMed=26197050; DOI=10.1371/journal.pone.0133033;
RA   Galka M.M., Rajagopalan N., Buhrow L.M., Nelson K.M., Switala J.,
RA   Cutler A.J., Palmer D.R., Loewen P.C., Abrams S.R., Loewen M.C.;
RT   "Identification of Interactions between Abscisic Acid and Ribulose-1,5-
RT   Bisphosphate Carboxylase/Oxygenase.";
RL   PLoS ONE 10:e0133033-e0133033(2015).
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 (Probable). Binds to abscisic acid
CC       (ABA); only half of the possible binding sites are occupied in the
CC       crystal; and there are indications this is a low affinity site
CC       (PubMed:26197050). {ECO:0000269|PubMed:26197050,
CC       ECO:0000305|PubMed:23295478, ECO:0000305|PubMed:26197050}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:23295478,
CC       ECO:0000269|PubMed:26197050}.
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, ECO:0000269|PubMed:23295478,
CC       ECO:0000269|PubMed:26197050}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR   EMBL; X04333; CAA27864.1; -; Genomic_DNA.
DR   EMBL; M21375; AAA33683.2; -; Genomic_DNA.
DR   PIR; A27874; RKPMS3.
DR   PDB; 4HHH; X-ray; 2.20 A; S/T/U/V=58-180.
DR   PDB; 4MKV; X-ray; 2.15 A; S/T/U/V=58-180.
DR   PDBsum; 4HHH; -.
DR   PDBsum; 4MKV; -.
DR   AlphaFoldDB; P07689; -.
DR   SMR; P07689; -.
DR   BRENDA; 4.1.1.39; 4872.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF19; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 2; 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; RuBisCO, small subunit; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Photorespiration; 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 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031542"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   HELIX           137..150
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   STRAND          155..162
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   TURN            163..166
FT                   /evidence="ECO:0007829|PDB:4MKV"
FT   STRAND          167..175
FT                   /evidence="ECO:0007829|PDB:4MKV"
SQ   SEQUENCE   180 AA;  20231 MW;  33DAD53A45C0CFE7 CRC64;
     MASMISSSAV TTVSRASTVQ SAAVAPFGGL KSMTGFPVKK VNTDITSITS NGGRVKCMQV
     WPPIGKKKFE TLSYLPPLTR DQLLKEVEYL LRKGWVPCLE FELEKGFVYR EHNKSPGYYD
     GRYWTMWKLP MFGTTDASQV LKELDEVVAA YPQAFVRIIG FDNVRQVQCI SFIAHTPESY
//