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Database: UniProt
Entry: P00873
LinkDB: P00873
Original site: P00873 
ID   RBS1_CHLRE              Reviewed;         185 AA.
AC   P00873;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-OCT-2017, entry version 132.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain 1, chloroplastic;
DE            Short=RuBisCO small subunit 1;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=RBCS-1;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   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
RT   encoding variant small subunits of ribulose bisphosphate
RT   carboxylase/oxygenase in Chlamydomonas reinhardtii.";
RL   J. Mol. Biol. 191:421-432(1986).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 46-185 OF HOLOENZYME IN
RP   COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP, SUBUNIT, AND
RP   METHYLATION AT MET-46.
RC   STRAIN=2137;
RX   PubMed=11641402; DOI=10.1074/jbc.M107765200;
RA   Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.;
RT   "First crystal structure of Rubisco from a green alga, Chlamydomonas
RT   reinhardtii.";
RL   J. Biol. Chem. 276:48159-48164(2001).
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
CC       at the same active site.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2).
CC   -!- SUBUNIT: 8 large chains + 8 small chains.
CC       {ECO:0000269|PubMed:11641402}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA28159.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; X04471; CAA28159.1; ALT_INIT; Genomic_DNA.
DR   PIR; A25785; RKKMS1.
DR   RefSeq; XP_001702409.1; XM_001702357.1.
DR   UniGene; Cre.3435; -.
DR   PDB; 1GK8; X-ray; 1.40 A; I/K/M/O=46-185.
DR   PDB; 1UW9; X-ray; 2.05 A; C/F/I/J/M/P/T/W=46-185.
DR   PDB; 1UWA; X-ray; 2.30 A; C/F/I/J/M/P/T/W=46-185.
DR   PDB; 1UZD; X-ray; 2.40 A; C/F/I/J/M/P/T/W=46-90, C/F/I/J/M/P/T/W=116-185.
DR   PDB; 1UZH; X-ray; 2.20 A; C/F/I/J/M/P/T/W=46-185.
DR   PDB; 2V63; X-ray; 1.80 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V67; X-ray; 2.00 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V68; X-ray; 2.30 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V69; X-ray; 2.80 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V6A; X-ray; 1.50 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2VDH; X-ray; 2.30 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2VDI; X-ray; 2.65 A; I/J/K/L/M/N/O/P=46-185.
DR   PDBsum; 1GK8; -.
DR   PDBsum; 1UW9; -.
DR   PDBsum; 1UWA; -.
DR   PDBsum; 1UZD; -.
DR   PDBsum; 1UZH; -.
DR   PDBsum; 2V63; -.
DR   PDBsum; 2V67; -.
DR   PDBsum; 2V68; -.
DR   PDBsum; 2V69; -.
DR   PDBsum; 2V6A; -.
DR   PDBsum; 2VDH; -.
DR   PDBsum; 2VDI; -.
DR   ProteinModelPortal; P00873; -.
DR   SMR; P00873; -.
DR   iPTMnet; P00873; -.
DR   PaxDb; P00873; -.
DR   PRIDE; P00873; -.
DR   EnsemblPlants; EDO96904; EDO96904; CHLREDRAFT_82986.
DR   GeneID; 5727949; -.
DR   Gramene; EDO96904; EDO96904; CHLREDRAFT_82986.
DR   KEGG; cre:CHLREDRAFT_82986; -.
DR   eggNOG; ENOG410IM2H; Eukaryota.
DR   eggNOG; COG4451; LUCA.
DR   KO; K01602; -.
DR   OMA; HECKQAY; -.
DR   EvolutionaryTrace; P00873; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.190.10; -; 1.
DR   InterPro; IPR024681; RuBisCO_sc.
DR   InterPro; IPR000894; RuBisCO_sc_dom.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
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; Carbon dioxide fixation; Chloroplast; Lyase;
KW   Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT       1     45       Chloroplast.
FT   CHAIN        46    185       Ribulose bisphosphate carboxylase small
FT                                chain 1, chloroplastic.
FT                                /FTId=PRO_0000031472.
FT   MOD_RES      46     46       N-methylmethionine.
FT                                {ECO:0000269|PubMed:11641402}.
FT   TURN         59     62       {ECO:0000244|PDB:1GK8}.
FT   HELIX        68     80       {ECO:0000244|PDB:1GK8}.
FT   STRAND       84     90       {ECO:0000244|PDB:1GK8}.
FT   HELIX        92     94       {ECO:0000244|PDB:1GK8}.
FT   HELIX       100    104       {ECO:0000244|PDB:1GK8}.
FT   STRAND      114    116       {ECO:0000244|PDB:2V6A}.
FT   STRAND      119    122       {ECO:0000244|PDB:1GK8}.
FT   HELIX       131    144       {ECO:0000244|PDB:1GK8}.
FT   STRAND      148    156       {ECO:0000244|PDB:1GK8}.
FT   TURN        157    160       {ECO:0000244|PDB:1GK8}.
FT   STRAND      161    169       {ECO:0000244|PDB:1GK8}.
FT   HELIX       180    182       {ECO:0000244|PDB:2V6A}.
SQ   SEQUENCE   185 AA;  20620 MW;  B4114FD98E807F16 CRC64;
     MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT PVNNKMFETF
     SYLPPLTDEQ IAAQVDYIVA NGWIPCLEFA EADKAYVSNE SAIRFGSVSC LYYDNRYWTM
     WKLPMFGCRD PMQVLREIVA CTKAFPDAYV RLVAFDNQKQ VQIMGFLVQR PKTARDFQPA
     NKRSV
//
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