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Database: UniProt/SWISS-PROT
Entry: RBS_SYNP6
LinkDB: RBS_SYNP6
Original site: RBS_SYNP6 
ID   RBS_SYNP6               Reviewed;         111 AA.
AC   P04716;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 129.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain;
DE            Short=RuBisCO small subunit;
DE            EC=4.1.1.39 {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445};
GN   Name=cbbS; Synonyms=rbcS; OrderedLocusNames=syc0129_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
OS   (Anacystis nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6415615; DOI=10.1093/nar/11.20.6957;
RA   Shinozaki K., Sugiura M.;
RT   "The gene for the small subunit of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase is located close to the gene for the large
RT   subunit in the cyanobacterium Anacystis nidulans 6301.";
RL   Nucleic Acids Res. 11:6957-6963(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shinozaki K., Sugiura M.;
RT   "Genes for the large and small subunits of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase constitute a single operon in a cyanobacterium
RT   Anacystis nidulans 6301.";
RL   Mol. Gen. Genet. 200:27-32(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular
RT   cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene
RT   content and organization.";
RL   Photosyn. Res. 93:55-67(2007).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA   Horken K.M., Tabita F.R.;
RT   "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT   molecules that possess different CO2/O2 substrate specificities.";
RL   Arch. Biochem. Biophys. 361:183-194(1999).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-110 OF ACTIVATED HOLOENZYME
RP   IN COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP, AND SUBUNIT.
RX   PubMed=8245022;
RA   Newman J., Gutteridge S.;
RT   "The X-ray structure of Synechococcus ribulose-bisphosphate
RT   carboxylase/oxygenase-activated quaternary complex at 2.2-A
RT   resolution.";
RL   J. Biol. Chem. 268:25876-25886(1993).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF INACTIVATED HOLOENZYME IN
RP   COMPLEX WITH PRODUCT ANALOG, FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RX   PubMed=7922027; DOI=10.1016/S0969-2126(00)00050-2;
RA   Newman J., Gutteridge S.;
RT   "Structure of an effector-induced inactivated state of ribulose 1,5-
RT   bisphosphate carboxylase/oxygenase: the binary complex between enzyme
RT   and xylulose 1,5-bisphosphate.";
RL   Structure 2:495-502(1994).
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. {ECO:0000269|PubMed:7922027,
CC       ECO:0000269|PubMed:9882445}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000269|PubMed:7922027,
CC       ECO:0000269|PubMed:9882445}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000269|PubMed:9882445}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=39 uM for ribulose 1,5-bisphosphate
CC         {ECO:0000269|PubMed:9882445};
CC         KM=173 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC         Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate
CC         {ECO:0000269|PubMed:9882445};
CC         Note=The CO(2)/O(2) specificity factor (tau) is 39.;
CC   -!- SUBUNIT: 8 large chains + 8 small chains.
CC       {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:8245022,
CC       ECO:0000305|PubMed:9882445}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
DR   EMBL; X03220; CAA26973.1; -; Genomic_DNA.
DR   EMBL; AP008231; BAD78319.1; -; Genomic_DNA.
DR   PIR; S07351; RKYCS.
DR   PDB; 1RBL; X-ray; 2.20 A; I/J/K/L/M/N/O/P=2-110.
DR   PDB; 1RSC; X-ray; 2.30 A; I/J/K/L/M/N/O/P=1-111.
DR   PDB; 1UZH; X-ray; 2.20 A; C/F/I/J/M/P/T/W=12-58, C/F/I/J/M/P/T/W=102-110.
DR   PDBsum; 1RBL; -.
DR   PDBsum; 1RSC; -.
DR   PDBsum; 1UZH; -.
DR   ProteinModelPortal; P04716; -.
DR   SMR; P04716; -.
DR   DIP; DIP-6211N; -.
DR   STRING; 269084.syc0129_c; -.
DR   EnsemblBacteria; BAD78319; BAD78319; syc0129_c.
DR   KEGG; syc:syc0129_c; -.
DR   eggNOG; COG4451; LUCA.
DR   HOGENOM; HOG000141332; -.
DR   KO; K01602; -.
DR   OMA; KQCQVLS; -.
DR   OrthoDB; POG091H13LH; -.
DR   SABIO-RK; P04716; -.
DR   EvolutionaryTrace; P04716; -.
DR   Proteomes; UP000001175; Chromosome.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.190.10; -; 1.
DR   InterPro; IPR000894; RuBisCO_sc_dom.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   Pfam; PF00101; RuBisCO_small; 1.
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;
KW   Complete proteome; Lyase; Monooxygenase; Oxidoreductase;
KW   Photosynthesis.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    111       Ribulose bisphosphate carboxylase small
FT                                chain.
FT                                /FTId=PRO_0000198624.
FT   REGION       12     21       Hydrophobic.
FT   TURN         14     17       {ECO:0000244|PDB:1RBL}.
FT   HELIX        23     36       {ECO:0000244|PDB:1RBL}.
FT   STRAND       39     46       {ECO:0000244|PDB:1RBL}.
FT   HELIX        68     81       {ECO:0000244|PDB:1RBL}.
FT   STRAND       85     93       {ECO:0000244|PDB:1RBL}.
FT   TURN         94     97       {ECO:0000244|PDB:1RBL}.
FT   STRAND       98    106       {ECO:0000244|PDB:1RBL}.
SQ   SEQUENCE   111 AA;  13333 MW;  F854F73FA70BD57B CRC64;
     MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP EEFYWTMWKL
     PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT VSFIVHRPGR Y
//
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