ID   RBS1_CHLRE              Reviewed;         185 AA.
AC   P00873; A8JGP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   Flags: Precursor;
GN   Name=RBCS1 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-1;
GN   ORFNames=CHLRE_02g120100v5 {ECO:0000305}, CHLREDRAFT_82986;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3820291; DOI=10.1016/0022-2836(86)90137-3;
RA   Goldschmidt-Clermont M., Rahire M.;
RT   "Sequence, evolution and differential expression of the two genes encoding
RT   variant small subunits of ribulose bisphosphate carboxylase/oxygenase in
RT   Chlamydomonas reinhardtii.";
RL   J. Mol. Biol. 191:421-432(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503, and cw92;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=28839179; DOI=10.1038/s41598-017-09473-x;
RA   Razzak M.A., Lee D.W., Yoo Y.J., Hwang I.;
RT   "Evolution of rubisco complex small subunit transit peptides from algae to
RT   plants.";
RL   Sci. Rep. 7:9279-9279(2017).
RN   [4] {ECO:0007744|PDB:1GK8}
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 46-185 OF HOLOENZYME IN COMPLEX
RP   WITH THE TRANSITION-STATE ANALOG 2-CABP, FUNCTION, SUBUNIT, AND METHYLATION
RP   AT MET-46.
RC   STRAIN=2137;
RX   PubMed=11641402; DOI=10.1074/jbc.m107765200;
RA   Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.;
RT   "First crystal structure of Rubisco from a green alga, Chlamydomonas
RT   reinhardtii.";
RL   J. Biol. Chem. 276:48159-48164(2001).
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:11641402}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:11641402}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00860, ECO:0000269|PubMed:28839179}.
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:11641402}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA28159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X04471; CAA28159.1; ALT_INIT; Genomic_DNA.
DR   EMBL; DS496186; EDO96904.1; -; Genomic_DNA.
DR   EMBL; CM008963; PNW87371.1; -; Genomic_DNA.
DR   PIR; A25785; RKKMS1.
DR   RefSeq; XP_001702409.1; XM_001702357.1.
DR   PDB; 1GK8; X-ray; 1.40 A; I/K/M/O=46-185.
DR   PDB; 1UW9; X-ray; 2.05 A; C/F/I/J/M/P/T/W=46-185.
DR   PDB; 1UWA; X-ray; 2.30 A; C/F/I/J/M/P/T/W=46-185.
DR   PDB; 1UZD; X-ray; 2.40 A; C/F/I/J/M/P/T/W=46-90, C/F/I/J/M/P/T/W=112-185.
DR   PDB; 1UZH; X-ray; 2.20 A; C/F/I/J/M/P/T/W=46-91, C/F/I/J/M/P/T/W=117-185.
DR   PDB; 2V63; X-ray; 1.80 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V67; X-ray; 2.00 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V68; X-ray; 2.30 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V69; X-ray; 2.80 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2V6A; X-ray; 1.50 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2VDH; X-ray; 2.30 A; I/J/K/L/M/N/O/P=46-185.
DR   PDB; 2VDI; X-ray; 2.65 A; I/J/K/L/M/N/O/P=46-185.
DR   PDBsum; 1GK8; -.
DR   PDBsum; 1UW9; -.
DR   PDBsum; 1UWA; -.
DR   PDBsum; 1UZD; -.
DR   PDBsum; 1UZH; -.
DR   PDBsum; 2V63; -.
DR   PDBsum; 2V67; -.
DR   PDBsum; 2V68; -.
DR   PDBsum; 2V69; -.
DR   PDBsum; 2V6A; -.
DR   PDBsum; 2VDH; -.
DR   PDBsum; 2VDI; -.
DR   AlphaFoldDB; P00873; -.
DR   SMR; P00873; -.
DR   STRING; 3055.P00873; -.
DR   iPTMnet; P00873; -.
DR   PaxDb; 3055-EDO96904; -.
DR   EnsemblPlants; PNW87371; PNW87371; CHLRE_02g120100v5.
DR   GeneID; 5727949; -.
DR   Gramene; PNW87371; PNW87371; CHLRE_02g120100v5.
DR   KEGG; cre:CHLRE_02g120100v5; -.
DR   eggNOG; ENOG502QTPB; Eukaryota.
DR   HOGENOM; CLU_098114_2_0_1; -.
DR   InParanoid; P00873; -.
DR   OMA; VIHISYT; -.
DR   OrthoDB; 5482775at2759; -.
DR   EvolutionaryTrace; P00873; -.
DR   Proteomes; UP000006906; Chromosome 2.
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-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; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF28; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 1; 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   3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Methylation; Photorespiration; Photosynthesis; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:11641402"
FT   CHAIN           46..185
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031472"
FT   MOD_RES         46
FT                   /note="N-methylmethionine"
FT                   /evidence="ECO:0000269|PubMed:11641402"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   HELIX           68..80
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   HELIX           100..104
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:2V6A"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   HELIX           131..144
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   STRAND          148..156
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   TURN            157..160
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   STRAND          161..169
FT                   /evidence="ECO:0007829|PDB:1GK8"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:2V6A"
SQ   SEQUENCE   185 AA;  20620 MW;  B4114FD98E807F16 CRC64;
     MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT PVNNKMFETF
     SYLPPLTDEQ IAAQVDYIVA NGWIPCLEFA EADKAYVSNE SAIRFGSVSC LYYDNRYWTM
     WKLPMFGCRD PMQVLREIVA CTKAFPDAYV RLVAFDNQKQ VQIMGFLVQR PKTARDFQPA
     NKRSV
//