ID RBS2B_ARATH Reviewed; 181 AA. AC P10797; Q9FF20; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit 2B, chloroplastic; DE Short=RuBisCO small subunit 2B; DE Flags: Precursor; GN Name=RBCS-2B; Synonyms=ATS2B; OrderedLocusNames=At5g38420; GN ORFNames=MXI10.14; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-100. RC STRAIN=cv. C24; TISSUE=Flower bud; RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). 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 -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00860}. 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. 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}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000255|HAMAP-Rule:MF_00860}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14564; CAA32701.1; -; Genomic_DNA. DR EMBL; AB005248; BAB09354.1; -; Genomic_DNA. DR EMBL; CP002688; AED94314.1; -; Genomic_DNA. DR EMBL; AY059939; AAL24421.1; -; mRNA. DR EMBL; AY062437; AAL32515.1; -; mRNA. DR EMBL; AY062458; AAL32536.1; -; mRNA. DR EMBL; AY062543; AAL32621.1; -; mRNA. DR EMBL; AY093288; AAM13287.1; -; mRNA. DR EMBL; BT002094; AAN72105.1; -; mRNA. DR EMBL; BT002554; AAO00914.1; -; mRNA. DR EMBL; BT003356; AAO29974.1; -; mRNA. DR EMBL; Z18199; CAA79132.1; -; mRNA. DR PIR; S03718; RKMUB2. DR RefSeq; NP_198658.1; NM_123203.5. DR AlphaFoldDB; P10797; -. DR SMR; P10797; -. DR BioGRID; 19080; 30. DR IntAct; P10797; 23. DR STRING; 3702.P10797; -. DR iPTMnet; P10797; -. DR PaxDb; 3702-AT5G38420-1; -. DR EnsemblPlants; AT5G38420.1; AT5G38420.1; AT5G38420. DR GeneID; 833829; -. DR Gramene; AT5G38420.1; AT5G38420.1; AT5G38420. DR KEGG; ath:AT5G38420; -. DR Araport; AT5G38420; -. DR TAIR; AT5G38420; RBCS2B. DR eggNOG; ENOG502QT0M; Eukaryota. DR HOGENOM; CLU_098114_1_0_1; -. DR InParanoid; P10797; -. DR OMA; NAWIRII; -. DR OrthoDB; 5482775at2759; -. DR PhylomeDB; P10797; -. DR BioCyc; MetaCyc:AT5G38420-MONOMER; -. DR PRO; PR:P10797; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P10797; 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:0022626; C:cytosolic ribosome; 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 Genevisible; P10797; AT. PE 2: Evidence at transcript level; KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration; KW Photosynthesis; Plastid; Reference proteome; 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 2B, FT chloroplastic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860" FT /id="PRO_0000031465" FT CONFLICT 6 FT /note="F -> L (in Ref. 1; CAA32701)" FT /evidence="ECO:0000305" SQ SEQUENCE 181 AA; 20350 MW; AB149EBBF84A1CC2 CRC64; MASSMFSSTA VVTSPAQATM VAPFTGLKSS ASFPVTRKAN NDITSITSNG GRVSCMKVWP PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE LEHGFVYREH GNTPGYYDGR YWTMWKLPLF GCTDSAQVLK EVEECKKEYP GAFIRIIGFD NTRQVQCISF IAYKPPSFTE A //