RBS1_LEMGI
ID RBS1_LEMGI Reviewed; 173 AA.
AC P00872;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit SSU1 {ECO:0000303|PubMed:2103442};
DE Flags: Precursor;
GN Name=RBCS1 {ECO:0000255|HAMAP-Rule:MF_00860};
GN Synonyms=SSU1 {ECO:0000303|PubMed:2103442};
OS Lemna gibba (Swollen duckweed).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Lemnoideae; Lemna.
OX NCBI_TaxID=4470;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=2103442; DOI=10.1007/bf00017723;
RA Silverthorne J., Wimpee C.F., Yamada T., Rolfe S.A., Tobin E.M.;
RT "Differential expression of individual genes encoding the small subunit of
RT ribulose-1,5-bisphosphate carboxylase in Lemna gibba.";
RL Plant Mol. Biol. 15:49-58(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6316282; DOI=10.1093/nar/11.22.8051;
RA Stiekema W.J., Wimpee C.F., Tobin E.M.;
RT "Nucleotide sequence encoding the precursor of the small subunit of
RT ribulose 1,5-bisphosphate carboxylase from Lemna gibba L.G-3.";
RL Nucleic Acids Res. 11:8051-8061(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 -!- INDUCTION: Accumulates to high levels when grown under continuous white
CC light. {ECO:0000269|PubMed:2103442}.
CC -!- MISCELLANEOUS: This protein is coded by one member of a small multigene
CC family.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24969.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17235; CAA35104.1; -; mRNA.
DR EMBL; X00137; CAA24969.1; ALT_INIT; mRNA.
DR PIR; A01091; RKDWS.
DR AlphaFoldDB; P00872; -.
DR SMR; P00872; -.
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..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 53..173
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031512"
FT CONFLICT 71..74
FT /note="LPPL -> FPLS (in Ref. 2; CAA24969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 173 AA; 19522 MW; D859F626DA009391 CRC64;
MMVSTAAVAR VRPAQTNMVG AFNGCRSSVA FPATRKANND LSTLPSSGGR VSCMQVWPPE
GLKKFETLSY LPPLSVEDLA KEVDYLLRND WVPCIEFSKE GFVYRENNAS PGYYDGRYWT
MWKLPMFGCT DASQVIAEVE EAKKAYPEYF VRIIGFDNKR QVQCISFIAY KPT
