ID   RBS1B_ARATH             Reviewed;         181 AA.
AC   P10796;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit 1B, chloroplastic {ECO:0000303|PubMed:9330910};
DE            Short=RuBisCO small subunit 1B;
DE   Flags: Precursor;
GN   Name=RBCS-1B {ECO:0000303|PubMed:9330910};
GN   Synonyms=ATS1B {ECO:0000303|Ref.1}; OrderedLocusNames=At5g38430;
GN   ORFNames=MXI10.15;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   INTERACTION WITH RBCX2.
RX   PubMed=21922322; DOI=10.1007/s11103-011-9823-8;
RA   Kolesinski P., Piechota J., Szczepaniak A.;
RT   "Initial characteristics of RbcX proteins from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 77:447-459(2011).
RN   [6] {ECO:0007744|PDB:5IU0}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH THE
RP   TRANSITION-STATE ANALOG 2-CABP, FUNCTION, AND SUBUNIT.
RX   PubMed=29372894; DOI=10.1107/s2059798317017132;
RA   Valegaard K., Hasse D., Andersson I., Gunn L.H.;
RT   "Structure of Rubisco from Arabidopsis thaliana in complex with 2-
RT   carboxyarabinitol-1,5-bisphosphate.";
RL   Acta Crystallogr. D 74:1-9(2018).
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 at
CC       the same active site. Although the small subunit is not catalytic it is
CC       essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00860,
CC       ECO:0000305|PubMed:29372894}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits
CC       (PubMed:29372894). Interacts with RBCX2 (PubMed:21922322).
CC       {ECO:0000269|PubMed:21922322, ECO:0000269|PubMed:29372894}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00860}.
CC   -!- MISCELLANEOUS: There are four genes coding for RBS in Arabidopsis
CC       thaliana. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:29372894}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR   EMBL; X14564; CAA32700.1; -; Genomic_DNA.
DR   EMBL; AB005248; BAB09355.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94315.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69887.1; -; Genomic_DNA.
DR   EMBL; AF410283; AAK95269.1; -; mRNA.
DR   EMBL; AY143814; AAN28753.1; -; mRNA.
DR   PIR; S03717; RKMUB1.
DR   RefSeq; NP_001318696.1; NM_001344249.1.
DR   RefSeq; NP_198659.1; NM_123204.4.
DR   PDB; 5IU0; X-ray; 1.50 A; I/J=1-181.
DR   PDBsum; 5IU0; -.
DR   AlphaFoldDB; P10796; -.
DR   SMR; P10796; -.
DR   BioGRID; 19081; 12.
DR   IntAct; P10796; 3.
DR   STRING; 3702.P10796; -.
DR   iPTMnet; P10796; -.
DR   PaxDb; 3702-AT5G38430-1; -.
DR   ProteomicsDB; 236531; -.
DR   EnsemblPlants; AT5G38430.1; AT5G38430.1; AT5G38430.
DR   EnsemblPlants; AT5G38430.2; AT5G38430.2; AT5G38430.
DR   GeneID; 833830; -.
DR   Gramene; AT5G38430.1; AT5G38430.1; AT5G38430.
DR   Gramene; AT5G38430.2; AT5G38430.2; AT5G38430.
DR   KEGG; ath:AT5G38430; -.
DR   Araport; AT5G38430; -.
DR   TAIR; AT5G38430; RBCS1B.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   HOGENOM; CLU_098114_1_0_1; -.
DR   InParanoid; P10796; -.
DR   OMA; SECKSAY; -.
DR   OrthoDB; 5482775at2759; -.
DR   PhylomeDB; P10796; -.
DR   BioCyc; MetaCyc:AT5G38430-MONOMER; -.
DR   PRO; PR:P10796; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P10796; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 1.
DR   HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR   InterPro; IPR024681; RuBisCO_ssu.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF29; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT 1A, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF12338; RbcS; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   PRINTS; PR00152; RUBISCOSMALL.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
DR   World-2DPAGE; 0003:P10796; -.
DR   Genevisible; P10796; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Photorespiration; Photosynthesis; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           55..181
FT                   /note="Ribulose bisphosphate carboxylase small subunit 1B,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031464"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   HELIX           78..90
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   HELIX           135..148
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   STRAND          152..160
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:5IU0"
FT   STRAND          165..173
FT                   /evidence="ECO:0007829|PDB:5IU0"
SQ   SEQUENCE   181 AA;  20286 MW;  63D5E3BA93E0B6CA CRC64;
     MASSMLSSAA VVTSPAQATM VAPFTGLKSS ASFPVTRKAN NDITSITSNG GRVSCMKVWP
     PIGKKKFETL SYLPDLTDVE LAKEVDYLLR NKWIPCVEFE LEHGFVYREH GNTPGYYDGR
     YWTMWKLPLF GCTDSAQVLK EVEECKKEYP GAFIRIIGFD NTRQVQCISF IAYKPPSFTD
     A
//