RBS3_PEA
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 25-MAY-2022, entry version 106.
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).
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: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 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
