RBS1_ACEAT
ID RBS1_ACEAT Reviewed; 182 AA.
AC P16134;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 95.
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 Flags: Precursor;
GN Name=RBCS1 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-1;
OS Acetabularia acetabulum (Mermaid's wine glass) (Acetabularia mediterranea).
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Dasycladales; Polyphysaceae; Acetabularia.
OX NCBI_TaxID=35845;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=17;
RX PubMed=2573818; DOI=10.1007/bf00332408;
RA Schneider S.U., Leible M.B., Yang X.P.;
RT "Strong homology between the small subunit of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase of two species of Acetabularia and the occurrence of
RT unusual codon usage.";
RL Mol. Gen. Genet. 218:445-452(1989).
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; X51811; CAA36108.1; -; mRNA.
DR PIR; S05349; RKJK1M.
DR AlphaFoldDB; P16134; -.
DR SMR; P16134; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; Lyase; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 43..182
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 1"
FT /id="PRO_0000031454"
SQ SEQUENCE 182 AA; 20659 MW; 40CC0CA4BD1824BD CRC64;
MASIMMNKSV VLSKECAKPL ATPKVTLNKR GFATTIATKN REMMVWQPFN NKMFETFSFL
PPLTDEQISK QVDYILTNSW TPCLEFAASD QAYAGNENCI RMGPVASTYQ DNRYWTMWKL
PMFGCTDGSQ VLSEIQACTK AFPDAYIRLV CFDANRQVQI SGFLVHRPPS ATDYRLPADR
QV
