RBS1_PEA
ID RBS1_PEA Reviewed; 136 AA.
AC P00868;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 102.
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 AltName: Full=PSSU1;
DE Flags: Precursor; Fragment;
GN Name=RBCS1 {ECO:0000255|HAMAP-Rule:MF_00860};
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 [MRNA].
RA Bedbrook J.R., Smith S.M., Ellis R.J.;
RT "Molecular cloning and sequencing of cDNA encoding the precursor to the
RT small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase.";
RL Nature 287:692-697(1980).
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; J01256; AAA33684.1; -; mRNA.
DR PIR; A01087; RKPMS.
DR AlphaFoldDB; P00868; -.
DR SMR; P00868; -.
DR DIP; DIP-609N; -.
DR IntAct; P00868; 2.
DR MINT; P00868; -.
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; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 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..13
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 14..136
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 1"
FT /id="PRO_0000031540"
FT NON_TER 1
SQ SEQUENCE 136 AA; 15883 MW; 87DD3BAAB37DC6F6 CRC64;
NTDITSNGER VKCMQVWPPI GKKKFETLSY LPPLTRDQLL KEVEYLLRKG WVPCLEFELL
KGFVYGEHNK SPRYYDGRYW TMWKLPMFGT TDPAQVVKEV DEVVAAYPEA FVRVIGFNNV
RQVQCISFIA HTPESY