ID RBS_MAIZE Reviewed; 170 AA.
AC P05348; Q43355;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 27-MAR-2024, entry version 147.
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 Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3436948; DOI=10.1093/oxfordjournals.jbchem.a122103;
RA Matsuoka M., Kano-Murakami Y., Tanaka Y., Ozeki Y., Ymamoto N.;
RT "Nucleotide sequence of cDNA encoding the small subunit of ribulose-1,5-
RT bisphosphate carboxylase from maize.";
RL J. Biochem. 102:673-676(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. F2;
RX PubMed=3588298; DOI=10.1093/nar/15.10.4360;
RA Lebrun M., Waksman G., Freyssinet G.;
RT "Nucleotide sequence of a gene encoding corn ribulose-1,5-bisphosphate
RT carboxylase/oxygenase small subunit (rbcs).";
RL Nucleic Acids Res. 15:4360-4360(1987).
RN [3]
RP PROTEIN SEQUENCE OF 48-170.
RX PubMed=3066367; DOI=10.1515/bchm3.1988.369.2.609;
RA Ren L., Salnikow J., Vater J.;
RT "Ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea mays: amino-acid
RT sequence of the small subunit.";
RL Biol. Chem. Hoppe-Seyler 369:609-615(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-10.
RX PubMed=1822995; DOI=10.1105/tpc.3.9.997;
RA Schaffner A.R., Sheen J.;
RT "Maize rbcS promoter activity depends on sequence elements not found in
RT dicot rbcS promoters.";
RL Plant Cell 3:997-1012(1991).
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; D00170; BAA00120.1; -; mRNA.
DR EMBL; X06535; CAA29784.1; -; mRNA.
DR EMBL; Y00322; CAA68419.1; -; Genomic_DNA.
DR EMBL; S42508; AAD13825.1; -; Genomic_DNA.
DR EMBL; S42568; AAD13826.1; -; Genomic_DNA.
DR PIR; S00534; RKZMS.
DR RefSeq; NP_001105294.1; NM_001111824.1.
DR AlphaFoldDB; P05348; -.
DR SMR; P05348; -.
DR STRING; 4577.P05348; -.
DR PaxDb; 4577-GRMZM2G098520_P01; -.
DR EnsemblPlants; Zm00001eb197410_T001; Zm00001eb197410_P001; Zm00001eb197410.
DR GeneID; 542212; -.
DR Gramene; Zm00001eb197410_T001; Zm00001eb197410_P001; Zm00001eb197410.
DR KEGG; zma:542212; -.
DR MaizeGDB; 62391; -.
DR eggNOG; ENOG502QT0M; Eukaryota.
DR HOGENOM; CLU_098114_1_0_1; -.
DR InParanoid; P05348; -.
DR OMA; FELGNPF; -.
DR OrthoDB; 5482775at2759; -.
DR SABIO-RK; P05348; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; P05348; baseline and differential.
DR Genevisible; P05348; ZM.
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:SF10; 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 Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Photorespiration; Photosynthesis; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:3066367"
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 47..170
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031522"
FT VARIANT 53
FT /note="A -> I"
FT VARIANT 81..82
FT /note="LR -> IV"
FT VARIANT 85
FT /note="W -> E"
FT VARIANT 92
FT /note="S -> V"
FT VARIANT 94
FT /note="V -> L"
FT VARIANT 124
FT /note="N -> T"
FT VARIANT 128
FT /note="Q -> L"
FT VARIANT 132
FT /note="E -> V"
FT VARIANT 138..139
FT /note="KS -> AA"
FT VARIANT 142
FT /note="D -> G"
FT VARIANT 153..154
FT /note="IK -> VR"
FT VARIANT 163
FT /note="A -> L"
FT VARIANT 165
FT /note="K -> G"
FT CONFLICT 81
FT /note="Missing (in Ref. 2; CAA68419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 170 AA; 19151 MW; 4625A5FDED3C2663 CRC64;
MAPTVMMASS ATAVAPFQGL KSTASLPVAR RSSRSLGNVS NGGRIRCMQV WPAYGNKKFE
TLSYLPPLST DDLLKQVDYL LRNGWIPCLE FSKVGFVYRE NSTSPCYYDG RYWTMWKLPM
FGCNDATQVY KELQEAIKSY PDAFHRVIGF DNIKQTQCVS FIAYKPPGSD
//
