RBS1_SPIOL
ID RBS1_SPIOL Reviewed; 123 AA.
AC P00870;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 123.
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};
GN Name=RBCS1 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP PROTEIN SEQUENCE.
RA Martin P.G.;
RT "Amino acid sequence of the small subunit of ribulose-1,5-bisphosphate
RT carboxylase from spinach.";
RL Aust. J. Plant Physiol. 6:401-408(1979).
RN [2]
RP SEQUENCE REVISION TO 68-70.
RA Martin P.G.;
RL Submitted (OCT-1982) to the PIR data bank.
RN [3] {ECO:0007744|PDB:1RBO, ECO:0007744|PDB:1RCO}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF INACTIVE HOLOENZYME IN COMPLEX
RP WITH INHIBITORS 4-CABP AND XUBP, FUNCTION, AND SUBUNIT.
RX PubMed=8955130; DOI=10.1074/jbc.271.51.32894;
RA Taylor T.C., Fothergill M.D., Andersson I.;
RT "A common structural basis for the inhibition of ribulose 1,5-bisphosphate
RT carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-
RT bisphosphate.";
RL J. Biol. Chem. 271:32894-32899(1996).
RN [4] {ECO:0007744|PDB:1RCX, ECO:0007744|PDB:1RXO}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH
RP SUBSTRATE AND CALCIUM IN ACTIVATED AND INACTIVATED STATE, FUNCTION, AND
RP SUBUNIT.
RX PubMed=9034362; DOI=10.1006/jmbi.1996.0738;
RA Taylor T.C., Andersson I.;
RT "The structure of the complex between rubisco and its natural substrate
RT ribulose 1,5-bisphosphate.";
RL J. Mol. Biol. 265:432-444(1997).
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:8955130}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:8955130}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|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:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:8955130}.
CC -!- MISCELLANEOUS: This protein is expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_00860}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The Plant Kingdom's sloth
CC - Issue 38 of September 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/038";
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DR PIR; A01089; RKSPS.
DR PDB; 1RBO; X-ray; 2.30 A; C/F/I/S=1-123.
DR PDB; 1RCO; X-ray; 2.30 A; C/F/I/M/P/S/T/W=1-123.
DR PDB; 1RCX; X-ray; 2.40 A; C/F/I/M/P/S/T/W=1-123.
DR PDB; 1RXO; X-ray; 2.20 A; C/F/I/S=1-123.
DR PDB; 8RUC; X-ray; 1.60 A; I/J/K/L=1-123.
DR PDBsum; 1RBO; -.
DR PDBsum; 1RCO; -.
DR PDBsum; 1RCX; -.
DR PDBsum; 1RXO; -.
DR PDBsum; 8RUC; -.
DR AlphaFoldDB; P00870; -.
DR SMR; P00870; -.
DR DIP; DIP-27640N; -.
DR IntAct; P00870; 1.
DR Allergome; 3814; Spi o RuBisCO.
DR BRENDA; 4.1.1.39; 5812.
DR EvolutionaryTrace; P00870; -.
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 Direct protein sequencing; Photorespiration; Photosynthesis; Plastid.
FT CHAIN 1..123
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 1"
FT /id="PRO_0000198589"
FT MOD_RES 1
FT /note="Methionine derivative"
FT VARIANT 94
FT /note="P -> Y"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:8RUC"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:8RUC"
SQ SEQUENCE 123 AA; 14283 MW; DC727DD6EF1EF59B CRC64;
MQVWPPLGLK KFETLSYLPP LTTEQLLAEV NYLLVKGWIP PLEFEVKDGF VYREHDKSPG
YYDGRYWTMW KLPMFGGTDP AQVVNEVEEV KKAPPDAFVR FIGFNDKREV QCISFIAYKP
AGY
