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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: RBS3B_ARATH B3H5S2_ARATH F4KA76_ARATH
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}.
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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
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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}.
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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
//
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