ID A9SCN2_PHYPA Unreviewed; 182 AA. AC A9SCN2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 104. 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=RBCS {ECO:0000256|HAMAP-Rule:MF_00860}; GN ORFNames=PHYPA_020104 {ECO:0000313|EMBL:PNR39824.1}, PHYPA_020105 GN {ECO:0000313|EMBL:PNR39825.1}; OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium. OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR39825.1}; RN [1] {ECO:0000313|EMBL:PNR39825.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_22720V3.1, RC ECO:0000313|Proteomes:UP000006727}; RX PubMed=18079367; DOI=10.1126/science.1150646; RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y., RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., RA Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the conquest RT of land by plants."; RL Science 319:64-69(2008). RN [2] {ECO:0000313|EMBL:PNR39825.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_22720V3.1, RC ECO:0000313|Proteomes:UP000006727}; RX PubMed=29237241; DOI=10.1111/tpj.13801; RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B., RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J., RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G., RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W., RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W., RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J., RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M., RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y., RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M., RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J., RA Schmutz J., Rensing S.A.; RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome RT structure and evolution."; RL Plant J. 93:515-533(2018). RN [3] {ECO:0000313|EnsemblPlants:Pp3c15_22720V3.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (DEC-2020) to UniProtKB. 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; ABEU02000015; PNR39824.1; -; Genomic_DNA. DR EMBL; ABEU02000015; PNR39825.1; -; Genomic_DNA. DR RefSeq; XP_001764106.1; XM_001764054.1. DR RefSeq; XP_001764179.1; XM_001764127.1. DR AlphaFoldDB; A9SCN2; -. DR SMR; A9SCN2; -. DR STRING; 3218.A9SCN2; -. DR PaxDb; 3218-PP1S66_47V6-1; -. DR EnsemblPlants; Pp3c15_22720V3.1; Pp3c15_22720V3.1; Pp3c15_22720. DR EnsemblPlants; Pp3c15_22720V3.2; Pp3c15_22720V3.2; Pp3c15_22720. DR EnsemblPlants; Pp3c15_22730V3.1; Pp3c15_22730V3.1; Pp3c15_22730. DR EnsemblPlants; Pp3c15_22730V3.2; Pp3c15_22730V3.2; Pp3c15_22730. DR Gramene; Pp3c15_22720V3.1; Pp3c15_22720V3.1; Pp3c15_22720. DR Gramene; Pp3c15_22720V3.2; Pp3c15_22720V3.2; Pp3c15_22720. DR Gramene; Pp3c15_22730V3.1; Pp3c15_22730V3.1; Pp3c15_22730. DR Gramene; Pp3c15_22730V3.2; Pp3c15_22730V3.2; Pp3c15_22730. DR eggNOG; ENOG502QT0M; Eukaryota. DR HOGENOM; CLU_098114_1_0_1; -. DR InParanoid; A9SCN2; -. DR OMA; CIAFIAY; -. DR OrthoDB; 5482775at2759; -. DR Proteomes; UP000006727; Chromosome 15. 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; IPR036385; RuBisCO_ssu_sf. DR PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31262:SF0; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT DOMAIN-CONTAINING PROTEIN; 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 3: Inferred from homology; 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 Reference proteome {ECO:0000313|Proteomes:UP000006727}. FT DOMAIN 72..181 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 182 AA; 19908 MW; EFCDACCBD8362312 CRC64; MASVVAASSV VAPATFVAAS SSVSNSKSNS VKAFSGLKSA TLFTSKAETL SSVQNGSRVQ CMQVWNPIGQ TKFETFSYLP PLSDDAIAKQ VEYMIQQKLI PCLEFDVNSN GVSRANNSSP GYYDGRYWTM WKLPMFGCQD SAQVLREIEE CKKTFPGCFV RVLGFDNVKQ VQICGFLVAR PN //