LinkDB: RBS3B_ARATH B3H5S2_ARATH F4KA76_ARATH
Original site: RBS3B_ARATH B3H5S2_ARATH F4KA76_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 24-JAN-2024, entry version 180. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit 3B, chloroplastic; DE Short=RuBisCO small subunit 3B; 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; 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). 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 -!- INTERACTION: CC P10798; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-639640, EBI-4426557; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP- CC Rule:MF_00860}. 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 -!- 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; 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 AlphaFoldDB; P10798; -. DR SMR; P10798; -. DR BioGRID; 19079; 12. DR IntAct; P10798; 6. DR STRING; 3702.P10798; -. DR iPTMnet; P10798; -. DR SWISS-2DPAGE; P99057; -. DR PaxDb; 3702-AT5G38410-3; -. 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 TAIR; AT5G38410; RBCS3B. DR eggNOG; ENOG502QT0M; Eukaryota. DR InParanoid; P10798; -. 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: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:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT 1B, 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. PE 1: Evidence at protein level; KW Alternative splicing; 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 3B, FT chloroplastic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860" FT /id="PRO_0000031466" FT CONFLICT 47 FT /note="A -> T (in Ref. 1; CAA32702)" FT /evidence="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 //
ID B3H5S2_ARATH Unreviewed; 186 AA. AC B3H5S2; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 24-JAN-2024, entry version 109. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860}; DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00860}; GN Name=RBCS3B {ECO:0000313|EMBL:AED94313.1, ECO:0000313|TAIR:AT5G38410}; GN Synonyms=MXI10.13 {ECO:0000313|EMBL:AED94313.1}, MXI10_13 GN {ECO:0000313|EMBL:AED94313.1}, RBCS {ECO:0000256|HAMAP-Rule:MF_00860}, GN Rubisco small subunit 3B {ECO:0000313|EMBL:AED94313.1}; GN OrderedLocusNames=At5g38410 {ECO:0000313|Araport:AT5G38410, GN ECO:0000313|EMBL:AED94313.1}; 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 {ECO:0000313|EMBL:AED94313.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AED94313.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130714; DOI=10.1038/35048507; RG Kazusa DNA Research Institute; RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium; RG European Union Arabidopsis Genome Sequencing Consortium; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D., RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B., RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."; RL Nature 408:823-826(2000). RN [2] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; 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). 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:0000256|HAMAP-Rule:MF_00860, CC ECO:0000256|RuleBase:RU003627}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_00860}. 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:0000256|HAMAP-Rule:MF_00860}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}. 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; CP002688; AED94313.1; -; Genomic_DNA. DR RefSeq; NP_001119331.1; NM_001125859.2. DR AlphaFoldDB; B3H5S2; -. DR SMR; B3H5S2; -. DR ProteomicsDB; 194069; -. DR EnsemblPlants; AT5G38410.3; AT5G38410.3; AT5G38410. DR GeneID; 833828; -. DR Gramene; AT5G38410.3; AT5G38410.3; AT5G38410. DR Araport; AT5G38410; -. DR TAIR; AT5G38410; RBCS3B. DR OMA; HRENGNS; -. DR OrthoDB; 5482775at2759; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; B3H5S2; 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:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule. DR GO; GO:0015979; P:photosynthesis; IMP:TAIR. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IMP:TAIR. 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:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT 1B, 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. PE 1: Evidence at protein level; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00860}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_00860}; KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}; KW Proteomics identification {ECO:0007829|PeptideAtlas:B3H5S2, KW ECO:0007829|ProteomicsDB:B3H5S2}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT DOMAIN 66..180 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 186 AA; 20840 MW; A03CB892CBE1299F CRC64; MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKTN KDITSIASNG GRVSCMKVWP PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE LEVINTKHGF VYREHGNTPG YYDGRYWTMW KLPLFGCTDS AQVLKEVEEC KKEYPGAFIR IIGFDNTRQV QCISFIAYKP PSFTEA //
ID F4KA76_ARATH Unreviewed; 174 AA. AC F4KA76; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 24-JAN-2024, entry version 74. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860}; DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00860}; GN Name=RBCS3B {ECO:0000313|EMBL:AED94312.1, ECO:0000313|TAIR:AT5G38410}; GN Synonyms=MXI10.13 {ECO:0000313|EMBL:AED94312.1}, MXI10_13 GN {ECO:0000313|EMBL:AED94312.1}, RBCS {ECO:0000256|HAMAP-Rule:MF_00860}, GN Rubisco small subunit 3B {ECO:0000313|EMBL:AED94312.1}; GN OrderedLocusNames=At5g38410 {ECO:0000313|Araport:AT5G38410, GN ECO:0000313|EMBL:AED94312.1}; 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 {ECO:0000313|EMBL:AED94312.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AED94312.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130714; DOI=10.1038/35048507; RG Kazusa DNA Research Institute; RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium; RG European Union Arabidopsis Genome Sequencing Consortium; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D., RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B., RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."; RL Nature 408:823-826(2000). RN [2] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; 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). 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:0000256|HAMAP-Rule:MF_00860, CC ECO:0000256|RuleBase:RU003627}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_00860}. 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:0000256|HAMAP-Rule:MF_00860}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}. 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; CP002688; AED94312.1; -; Genomic_DNA. DR RefSeq; NP_001031981.1; NM_001036904.1. DR AlphaFoldDB; F4KA76; -. DR SMR; F4KA76; -. DR ProteomicsDB; 195795; -. DR EnsemblPlants; AT5G38410.2; AT5G38410.2; AT5G38410. DR GeneID; 833828; -. DR Gramene; AT5G38410.2; AT5G38410.2; AT5G38410. DR Araport; AT5G38410; -. DR TAIR; AT5G38410; RBCS3B. DR HOGENOM; CLU_098114_1_0_1; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; F4KA76; baseline and differential. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule. 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:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT 1B, 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. PE 1: Evidence at protein level; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00860}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_00860}; KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F4KA76, KW ECO:0007829|ProteomicsDB:F4KA76}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT DOMAIN 66..168 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 174 AA; 19395 MW; AB2D5BC014ACE539 CRC64; MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKTN KDITSIASNG GRVSCMKVWP PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE LEHGNTPGYY DGRYWTMWKL PLFGCTDSAQ VLKEVEECKK EYPGAFIRII GFDNTRQVQC ISFIAYKPPS FTEA //