RBS2_CHLRE
ID RBS2_CHLRE Reviewed; 185 AA.
AC P08475;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Flags: Precursor;
GN Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-2;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3820291; DOI=10.1016/0022-2836(86)90137-3;
RA Goldschmidt-Clermont M., Rahire M.;
RT "Sequence, evolution and differential expression of the two genes encoding
RT variant small subunits of ribulose bisphosphate carboxylase/oxygenase in
RT Chlamydomonas reinhardtii.";
RL J. Mol. Biol. 191:421-432(1986).
RN [2]
RP PROTEIN SEQUENCE OF 25-60.
RX PubMed=8223627; DOI=10.1111/j.1432-1033.1993.tb18335.x;
RA Su Q., Boschetti A.;
RT "Partial purification and properties of enzymes involved in the processing
RT of a chloroplast import protein from Chlamydomonas reinhardii.";
RL Eur. J. Biochem. 217:1039-1047(1993).
RN [3] {ECO:0007744|PDB:1IR2}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 46-185 OF ACTIVATED HOLOENZYME IN
RP COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND METHYLATION AT MET-46.
RC STRAIN=137c / CC-125;
RX PubMed=11866526; DOI=10.1006/jmbi.2001.5381;
RA Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J.,
RA Kato K., Shibata N., Inoue T., Yokota A., Kai Y.;
RT "Crystal structure of activated ribulose-1,5-bisphosphate
RT carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed
RT with 2-carboxyarabinitol-1,5-bisphosphate.";
RL J. Mol. Biol. 316:679-691(2002).
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 ECO:0000269|PubMed:11866526}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:11866526}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_00860, ECO:0000305|PubMed:11866526}. Plastid, chloroplast
CC stroma {ECO:0000305|PubMed:11866526}.
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, ECO:0000269|PubMed:11866526}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR EMBL; X04472; CAA28160.1; -; Genomic_DNA.
DR PIR; B25785; RKKMS2.
DR PDB; 1IR2; X-ray; 1.84 A; 1/2/3/4/5/6/7/8/I/J/K/L/M/N/O/P=46-185.
DR PDB; 1UZH; X-ray; 2.20 A; C/F/I/J/M/P/T/W=-.
DR PDB; 7JFO; EM; 2.13 A; B/D/F/H/J/L/N/P=1-185.
DR PDB; 7JN4; EM; 2.68 A; B/D/F/H/J/L/N/P=1-185.
DR PDB; 7JSX; EM; 2.06 A; B/D/F/H/J/L/N/P=1-185.
DR PDBsum; 1IR2; -.
DR PDBsum; 1UZH; -.
DR PDBsum; 7JFO; -.
DR PDBsum; 7JN4; -.
DR PDBsum; 7JSX; -.
DR AlphaFoldDB; P08475; -.
DR SMR; P08475; -.
DR iPTMnet; P08475; -.
DR EnsemblPlants; PNW87372; PNW87372; CHLRE_02g120150v5.
DR Gramene; PNW87372; PNW87372; CHLRE_02g120150v5.
DR OMA; RKNWVPC; -.
DR BRENDA; 4.1.1.39; 1318.
DR EvolutionaryTrace; P08475; -.
DR GO; GO:0009570; C:chloroplast stroma; 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 1: Evidence at protein level;
KW 3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Methylation; Photorespiration; Photosynthesis;
KW Plastid; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11866526"
FT CHAIN 46..185
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031473"
FT MOD_RES 46
FT /note="N-methylmethionine"
FT /evidence="ECO:0000269|PubMed:11866526"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:1IR2"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1IR2"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1IR2"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1IR2"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1IR2"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:7JSX"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:1IR2"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1IR2"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1IR2"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:1IR2"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1IR2"
SQ SEQUENCE 185 AA; 20647 MW; E19A3627EF484F50 CRC64;
MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT PVNNKMFETF
SYLPPLSDEQ IAAQVDYIVA NGWIPCLEFA ESDKAYVSNE SAIRFGSVSC LYYDNRYWTM
WKLPMFGCRD PMQVLREIVA CTKAFPDAYV RLVAFDNQKQ VQIMGFLVQR PKSARDWQPA
NKRSV
