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Database: UniProt
Entry: Q43832
LinkDB: Q43832
Original site: Q43832 
ID   RBS2_SPIOL              Reviewed;         180 AA.
AC   Q43832;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-MAY-2018, entry version 118.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain 2, chloroplastic;
DE            Short=RuBisCO small subunit 2;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=RBCS2;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae;
OC   Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nobel; TISSUE=Leaf;
RA   Diogon T., Capelli N., Greppin H., Simon P.;
RT   "cDNA cloning and expression of a ribulose-1,5-bisphophate carboxylase
RT   small subunit precursor in Spinacia oleracea.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATED HOLOENZYME IN
RP   COMPLEX WITH TRANSITION-STATE ANALOG, AND SUBUNIT.
RX   PubMed=17740342; DOI=10.1126/science.244.4905.702;
RA   Knight S., Andersson I., Braenden C.-I.;
RT   "Reexamination of the three-dimensional structure of the small subunit
RT   of RuBisCo from higher plants.";
RL   Science 244:702-705(1989).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF ACTIVATED HOLOENZYME IN
RP   COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM.
RX   PubMed=2118958; DOI=10.1016/S0022-2836(05)80100-7;
RA   Knight S., Andersson I., Braenden C.-I.;
RT   "Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase
RT   from spinach at 2.4-A resolution. Subunit interactions and active
RT   site.";
RL   J. Mol. Biol. 215:113-160(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-123 OF INACTIVE HOLOENZYME
RP   IN COMPLEX WITH INHIBITORS 4-CABP AND XUBP, AND SUBUNIT.
RX   PubMed=8955130; DOI=10.1074/jbc.271.51.32894;
RA   Taylor T.C., Fothergill M.D., Andersson I.;
RT   "A common structural basis for the inhibition of ribulose 1,5-
RT   bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and
RT   xylulose 1,5-bisphosphate.";
RL   J. Biol. Chem. 271:32894-32899(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF ACTIVATED HOLOENZYME IN
RP   COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, AND
RP   SUBUNIT.
RX   PubMed=8648644; DOI=10.1006/jmbi.1996.0310;
RA   Andersson I.;
RT   "Large structures at high resolution: the 1.6-A crystal structure of
RT   spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with
RT   2-carboxyarabinitol bisphosphate.";
RL   J. Mol. Biol. 259:160-174(1996).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 58-180 OF ACTIVATED
RP   HOLOENZYME IN COMPLEX WITH 3-PHOSPHOGLYCERATE AND MAGNESIUM, AND
RP   SUBUNIT.
RX   PubMed=9092835; DOI=10.1021/bi962818w;
RA   Taylor T.C., Andersson I.;
RT   "Structure of a product complex of spinach ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase.";
RL   Biochemistry 36:4041-4046(1997).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH
RP   SUBSTRATE AND CALCIUM IN ACTIVATED AND INACTIVATED STATE, AND SUBUNIT.
RX   PubMed=9034362; DOI=10.1006/jmbi.1996.0738;
RA   Taylor T.C., Andersson I.;
RT   "The structure of the complex between rubisco and its natural
RT   substrate ribulose 1,5-bisphosphate.";
RL   J. Mol. Biol. 265:432-444(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 58-180 OF HOLOENZYME IN
RP   COMPLEX WITH TRANSITION STATE ANALOG 2-CABP AND CALCIUM.
RX   PubMed=14596800; DOI=10.1016/j.jmb.2003.09.025;
RA   Karkehabadi S., Taylor T.C., Andersson I.;
RT   "Calcium supports loop closure but not catalysis in Rubisco.";
RL   J. Mol. Biol. 334:65-73(2003).
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:14596800, ECO:0000269|PubMed:17740342,
CC       ECO:0000269|PubMed:8648644, ECO:0000269|PubMed:8955130,
CC       ECO:0000269|PubMed:9034362, ECO:0000269|PubMed:9092835}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The Plant Kingdom's
CC       sloth - Issue 38 of September 2003;
CC       URL="https://web.expasy.org/spotlight/back_issues/038";
DR   EMBL; X97600; CAA66201.1; -; mRNA.
DR   PIR; S78083; S78083.
DR   PDB; 1AA1; X-ray; 2.20 A; C/F/I/S=58-180.
DR   PDB; 1AUS; X-ray; 2.20 A; S/T/U/V=58-180.
DR   PDB; 1IR1; X-ray; 1.80 A; S/T/U/V=58-180.
DR   PDB; 1UPM; X-ray; 2.30 A; C/F/I/M/P/S/T/W=58-180.
DR   PDB; 1UPP; X-ray; 2.30 A; I/J/K/L=58-180.
DR   PDB; 1UZD; X-ray; 2.40 A; C/F/I/J/M/P/T/W=103-121.
DR   PDBsum; 1AA1; -.
DR   PDBsum; 1AUS; -.
DR   PDBsum; 1IR1; -.
DR   PDBsum; 1UPM; -.
DR   PDBsum; 1UPP; -.
DR   PDBsum; 1UZD; -.
DR   ProteinModelPortal; Q43832; -.
DR   SMR; Q43832; -.
DR   IntAct; Q43832; 1.
DR   MINT; Q43832; -.
DR   PRIDE; Q43832; -.
DR   EvolutionaryTrace; Q43832; -.
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; 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   1: Evidence at protein level;
KW   3D-structure; Carbon dioxide fixation; Chloroplast; Lyase;
KW   Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis;
KW   Plastid; Transit peptide.
FT   TRANSIT       1     57       Chloroplast. {ECO:0000250}.
FT   CHAIN        58    180       Ribulose bisphosphate carboxylase small
FT                                chain 2, chloroplastic.
FT                                /FTId=PRO_0000031558.
FT   TURN         71     74       {ECO:0000244|PDB:1IR1}.
FT   HELIX        80     92       {ECO:0000244|PDB:1IR1}.
FT   STRAND       96    104       {ECO:0000244|PDB:1IR1}.
FT   STRAND      125    128       {ECO:0000244|PDB:1IR1}.
FT   HELIX       137    150       {ECO:0000244|PDB:1IR1}.
FT   STRAND      154    162       {ECO:0000244|PDB:1IR1}.
FT   TURN        163    166       {ECO:0000244|PDB:1IR1}.
FT   STRAND      167    175       {ECO:0000244|PDB:1IR1}.
SQ   SEQUENCE   180 AA;  20326 MW;  651FF2F212CFD64A CRC64;
     MASSVLSSAA VATVSRTPAQ ASMVAPFTGL KSTVGFPATK KNDDITSLAS NGGRVQCMKV
     WPTQNMKRYE TLSYLPPLTT DQLARQVDYL LNNKWVPCLE FETDHGFVYR EHHNSPGYYD
     GRYWTMWKLP MFGCTDPAQV LNELEECKKE YPNAFIRIIG FDSNRQVQCV SFIAYKPAGY
//
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