RBS1B_ARATH
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 03-AUG-2022, entry version 170.
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.AT5G38430.1; -.
DR iPTMnet; P10796; -.
DR World-2DPAGE; 0003:P10796; -.
DR PaxDb; P10796; -.
DR PRIDE; P10796; -.
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; locus:2177406; AT5G38430.
DR eggNOG; ENOG502QT0M; Eukaryota.
DR HOGENOM; CLU_098114_1_0_1; -.
DR InParanoid; P10796; -.
DR OMA; RKNWVPC; -.
DR OrthoDB; 1258997at2759; -.
DR PhylomeDB; P10796; -.
DR BioCyc; MetaCyc:AT5G38430-MON; -.
DR PRO; PR:P10796; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P10796; baseline and differential.
DR Genevisible; P10796; AT.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 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; PTHR31262; 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; SSF55239; 1.
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
