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Database: UniProt/SWISS-PROT
Entry: RBS1_NICSY
LinkDB: RBS1_NICSY
Original site: RBS1_NICSY 
ID   RBS1_NICSY              Reviewed;         180 AA.
AC   P69250; P00866; P00867; P26666;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   28-FEB-2018, entry version 52.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain, chloroplastic;
DE            Short=RuBisCO small subunit;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=RBCS;
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae;
OC   Nicotianoideae; Nicotianeae; Nicotiana.
OX   NCBI_TaxID=4096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6549380; DOI=10.1016/0300-9084(84)90148-2;
RA   Pinck M., Guilley E., Durr A., Hoff M., Pinck L., Fleck J.;
RT   "Complete sequence of one of the mRNAs coding for the small subunit of
RT   ribulose bisphosphate carboxylase of Nicotiana sylvestris.";
RL   Biochimie 66:539-545(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 95-180.
RA   Pinck L., Fleck J., Pinck M., Hadidane R., Hirth L.;
RT   "Sequence of a cDNA clone encoding part of the small subunit of the
RT   ribulose-1,5-bisphosphate carboxylase of Nicotiana sylvestris.";
RL   FEBS Lett. 154:145-148(1983).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
DR   EMBL; X01722; CAA25862.1; -; mRNA.
DR   EMBL; J01308; AAA34111.1; -; mRNA.
DR   PIR; A01085; RKNTSS.
DR   RefSeq; XP_009772497.1; XM_009774195.1.
DR   RefSeq; XP_009795055.1; XM_009796753.1.
DR   RefSeq; XP_009795056.1; XM_009796754.1.
DR   ProteinModelPortal; P69250; -.
DR   SMR; P69250; -.
DR   GeneID; 104222872; -.
DR   GeneID; 104241798; -.
DR   GeneID; 104241799; -.
DR   KEGG; nsy:104222872; -.
DR   KEGG; nsy:104241798; -.
DR   KEGG; nsy:104241799; -.
DR   KO; K01602; -.
DR   Proteomes; UP000189701; Genome assembly.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.190.10; -; 1.
DR   InterPro; IPR024681; RuBisCO_sc.
DR   InterPro; IPR000894; RuBisCO_sc_dom.
DR   InterPro; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   Pfam; PF12338; RbcS; 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; Complete proteome;
KW   Lyase; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT       1     57       Chloroplast. {ECO:0000250}.
FT   CHAIN        58    180       Ribulose bisphosphate carboxylase small
FT                                chain, chloroplastic.
FT                                /FTId=PRO_0000031535.
SQ   SEQUENCE   180 AA;  20311 MW;  26CF3F48EF0860AD CRC64;
     MASSVLSSAA VATRSNVAQA NMVAPFTGLK SAASFPVSRK QNLDITSIAS NGGRVQCMQV
     WPPINKKKYE TLSYLPDLSQ EQLLSEVEYL LKNGWVPCLE FETEHGFVYR ENNKSPGYYD
     GRYWTMWKLP MFGCTDATQV LAEVEEAKKA YPQAWIRIIG FDNVRQVQCI SFIAYKPEGY
//
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