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Database: UniProt/SWISS-PROT
Entry: RBS3B_ARATH
LinkDB: RBS3B_ARATH
Original site: RBS3B_ARATH 
ID   RBS3B_ARATH             Reviewed;         181 AA.
AC   P10798; Q9FF21;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   20-DEC-2017, entry version 154.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain 3B, chloroplastic;
DE            Short=RuBisCO small subunit 3B;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=RBCS-3B; Synonyms=ATS3B; OrderedLocusNames=At5g38410;
GN   ORFNames=MXI10.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Columbia K85;
RX   AGRICOLA=IND91035191; DOI=10.1007/BF00019515;
RA   Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.;
RT   "Four genes in two diverged subfamilies encode the ribulose-1,5-
RT   bisphosphate carboxylase small subunit polypeptides of Arabidopsis
RT   thaliana.";
RL   Plant Mol. Biol. 11:745-759(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned
RT   P1 clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(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 (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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P10798-1; Sequence=Displayed;
CC   -!- MISCELLANEOUS: There are four genes coding for RBS in Arabidopsis
CC       thaliana.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
DR   EMBL; X14564; CAA32702.1; -; Genomic_DNA.
DR   EMBL; AB005248; BAB09353.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94311.1; -; Genomic_DNA.
DR   EMBL; AF360124; AAK25834.1; -; mRNA.
DR   EMBL; AY054552; AAK96743.1; -; mRNA.
DR   EMBL; AY051025; AAK93702.1; -; mRNA.
DR   EMBL; AF410314; AAK95300.1; -; mRNA.
DR   EMBL; AF462822; AAL58912.1; -; mRNA.
DR   EMBL; AY064686; AAL47390.1; -; mRNA.
DR   EMBL; AY098970; AAM19980.1; -; mRNA.
DR   EMBL; BT000721; AAN31863.1; -; mRNA.
DR   PIR; S03719; RKMUB3.
DR   RefSeq; NP_198657.1; NM_123202.4. [P10798-1]
DR   UniGene; At.20381; -.
DR   UniGene; At.24772; -.
DR   UniGene; At.46639; -.
DR   UniGene; At.49098; -.
DR   UniGene; At.49366; -.
DR   UniGene; At.70032; -.
DR   UniGene; At.70053; -.
DR   UniGene; At.71313; -.
DR   UniGene; At.74604; -.
DR   UniGene; At.75410; -.
DR   UniGene; At.75674; -.
DR   ProteinModelPortal; P10798; -.
DR   SMR; P10798; -.
DR   BioGrid; 19079; 6.
DR   IntAct; P10798; 5.
DR   STRING; 3702.AT5G38410.3; -.
DR   iPTMnet; P10798; -.
DR   SWISS-2DPAGE; P99057; -.
DR   PaxDb; P10798; -.
DR   PRIDE; P10798; -.
DR   EnsemblPlants; AT5G38410.1; AT5G38410.1; AT5G38410. [P10798-1]
DR   GeneID; 833828; -.
DR   Gramene; AT5G38410.1; AT5G38410.1; AT5G38410. [P10798-1]
DR   KEGG; ath:AT5G38410; -.
DR   Araport; AT5G38410; -.
DR   eggNOG; ENOG410IM2H; Eukaryota.
DR   eggNOG; COG4451; LUCA.
DR   HOGENOM; HOG000141332; -.
DR   InParanoid; P10798; -.
DR   KO; K01602; -.
DR   PhylomeDB; P10798; -.
DR   BioCyc; MetaCyc:AT5G38410-MONOMER; -.
DR   PRO; PR:P10798; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P10798; baseline and differential.
DR   Genevisible; P10798; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
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   Alternative splicing; Calvin cycle; Carbon dioxide fixation;
KW   Chloroplast; Complete proteome; Lyase; Monooxygenase; Oxidoreductase;
KW   Photorespiration; Photosynthesis; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     55       Chloroplast.
FT   CHAIN        56    181       Ribulose bisphosphate carboxylase small
FT                                chain 3B, chloroplastic.
FT                                /FTId=PRO_0000031466.
FT   CONFLICT     47     47       A -> T (in Ref. 1; CAA32702).
FT                                {ECO:0000305}.
SQ   SEQUENCE   181 AA;  20284 MW;  9A5688A9D055254D CRC64;
     MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKTN KDITSIASNG GRVSCMKVWP
     PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE LEHGFVYREH GNTPGYYDGR
     YWTMWKLPLF GCTDSAQVLK EVEECKKEYP GAFIRIIGFD NTRQVQCISF IAYKPPSFTE
     A
//
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