RBS1_CHLRE
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 03-AUG-2022, entry version 154.
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.EDO96904; -.
DR iPTMnet; P00873; -.
DR PRIDE; P00873; -.
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 OMA; IARQIDY; -.
DR OrthoDB; 1258997at2759; -.
DR EvolutionaryTrace; P00873; -.
DR Proteomes; UP000006906; Chromosome 2.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 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; PTHR31262; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 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
