RBS5_ACEPE
ID RBS5_ACEPE Reviewed; 184 AA.
AC P16133;
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 5 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 5 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Flags: Precursor;
GN Name=RBCS5 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-5;
OS Acetabularia peniculus (Green alga) (Polyphysa peniculus).
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Dasycladales; Polyphysaceae; Acetabularia.
OX NCBI_TaxID=35862;
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; X51810; CAA36107.1; -; mRNA.
DR PIR; S05354; RKJK5C.
DR AlphaFoldDB; P16133; -.
DR SMR; P16133; -.
DR PRIDE; P16133; -.
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..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 44..184
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031451"
SQ SEQUENCE 184 AA; 20684 MW; E0EE836A13DC25AD CRC64;
MAAAMMNKTI VVSKDGCARS SSIPKVATNK MGFASAVAMK KSREMMVWQP FNNKMFETFS
YLPPLTDEQI SKQVDYILAN SWTPCLEFAA SDQAYAGNEN CIRMGPVAST YQDNRYWTMW
KLPMFGCTDG SQVLSEIQAC TKAFPDAYIR LVCFDANRQV QISGFLVHRP PTATDYRLPA
DRQV
