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Database: UniProt/SWISS-PROT
Entry: RBS_NOSS1
LinkDB: RBS_NOSS1
Original site: RBS_NOSS1 
ID   RBS_NOSS1               Reviewed;         109 AA.
AC   P06514;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   05-DEC-2018, entry version 107.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain;
DE            Short=RuBisCO small subunit;
DE            EC=4.1.1.39;
GN   Name=cbbS; Synonyms=rbcS; OrderedLocusNames=alr1526;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6091125; DOI=10.1073/pnas.81.19.5961;
RA   Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R.;
RT   "Cotranscription of genes encoding the small and large subunits of
RT   ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena
RT   7120.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 3-phospho-D-glycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC   -!- SUBUNIT: 8 large chains + 8 small chains.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
DR   EMBL; J01540; AAA22042.1; -; Genomic_DNA.
DR   EMBL; L02520; AAA22025.1; -; Genomic_DNA.
DR   EMBL; L02521; AAA22026.1; -; Genomic_DNA.
DR   EMBL; L02522; AAA22030.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77892.1; -; Genomic_DNA.
DR   PIR; AH1996; AH1996.
DR   RefSeq; WP_010995695.1; NC_003272.1.
DR   ProteinModelPortal; P06514; -.
DR   SMR; P06514; -.
DR   STRING; 103690.alr1526; -.
DR   EnsemblBacteria; BAB77892; BAB77892; BAB77892.
DR   KEGG; ana:alr1526; -.
DR   eggNOG; ENOG4108VFZ; Bacteria.
DR   eggNOG; COG4451; LUCA.
DR   KO; K01602; -.
DR   OMA; KQCQVLS; -.
DR   OrthoDB; POG091H13LH; -.
DR   Proteomes; UP000002483; 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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Monooxygenase; Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN         1    109       Ribulose bisphosphate carboxylase small
FT                                chain.
FT                                /FTId=PRO_0000198610.
SQ   SEQUENCE   109 AA;  12827 MW;  00AF32BB0A703595 CRC64;
     MQTLPKERRY ETLSYLPPLT DVQIEKQVQY ILSQGYIPAV EFNEVSEPTE LYWTLWKLPL
     FGAKTSREVL AEVQSCRSQY PGHYIRVVGF DNIKQCQILS FIVHKPSRY
//
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