RBS2_SPIOL
ID RBS2_SPIOL Reviewed; 180 AA.
AC Q43832;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Flags: Precursor;
GN Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860};
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 NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nobel; TISSUE=Leaf;
RA Diogon T., Capelli N., Greppin H., Simon P.;
RT "cDNA cloning and expression of a ribulose-1,5-bisphophate carboxylase
RT small subunit precursor in Spinacia oleracea.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH TRANSITION-STATE ANALOG, AND SUBUNIT.
RX PubMed=17740342; DOI=10.1126/science.244.4905.702;
RA Knight S., Andersson I., Braenden C.-I.;
RT "Reexamination of the three-dimensional structure of the small subunit of
RT RuBisCo from higher plants.";
RL Science 244:702-705(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM.
RX PubMed=2118958; DOI=10.1016/s0022-2836(05)80100-7;
RA Knight S., Andersson I., Braenden C.-I.;
RT "Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from
RT spinach at 2.4-A resolution. Subunit interactions and active site.";
RL J. Mol. Biol. 215:113-160(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-123 OF INACTIVE HOLOENZYME IN
RP COMPLEX WITH INHIBITORS 4-CABP AND XUBP, 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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH THE TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, AND SUBUNIT.
RX PubMed=8648644; DOI=10.1006/jmbi.1996.0310;
RA Andersson I.;
RT "Large structures at high resolution: the 1.6-A crystal structure of
RT spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-
RT carboxyarabinitol bisphosphate.";
RL J. Mol. Biol. 259:160-174(1996).
RN [6] {ECO:0007744|PDB:1AA1, ECO:0007744|PDB:1AUS}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 58-180 OF ACTIVATED HOLOENZYME IN
RP COMPLEX WITH 3-PHOSPHOGLYCERATE AND MAGNESIUM, AND SUBUNIT.
RX PubMed=9092835; DOI=10.1021/bi962818w;
RA Taylor T.C., Andersson I.;
RT "Structure of a product complex of spinach ribulose-1,5-bisphosphate
RT carboxylase/oxygenase.";
RL Biochemistry 36:4041-4046(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH
RP SUBSTRATE AND CALCIUM IN ACTIVATED AND INACTIVATED STATE, AND 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).
RN [8] {ECO:0007744|PDB:1UPM, ECO:0007744|PDB:1UPP}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 58-180 OF HOLOENZYME IN COMPLEX
RP WITH TRANSITION STATE ANALOG 2-CABP AND CALCIUM.
RX PubMed=14596800; DOI=10.1016/j.jmb.2003.09.025;
RA Karkehabadi S., Taylor T.C., Andersson I.;
RT "Calcium supports loop closure but not catalysis in Rubisco.";
RL J. Mol. Biol. 334:65-73(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 ECO:0000305|PubMed:14596800, ECO:0000305|PubMed:17740342,
CC ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:8648644,
CC ECO:0000305|PubMed:8955130, ECO:0000305|PubMed:9034362,
CC ECO:0000305|PubMed:9092835}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:14596800,
CC ECO:0000269|PubMed:17740342, ECO:0000269|PubMed:8648644,
CC ECO:0000269|PubMed:8955130, ECO:0000269|PubMed:9034362,
CC ECO:0000269|PubMed:9092835}.
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:14596800,
CC ECO:0000269|PubMed:17740342, ECO:0000269|PubMed:8648644,
CC ECO:0000269|PubMed:8955130, ECO:0000269|PubMed:9034362,
CC ECO:0000269|PubMed:9092835}.
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 EMBL; X97600; CAA66201.1; -; mRNA.
DR PIR; S78083; S78083.
DR PDB; 1AA1; X-ray; 2.20 A; C/F/I/S=58-180.
DR PDB; 1AUS; X-ray; 2.20 A; S/T/U/V=58-180.
DR PDB; 1IR1; X-ray; 1.80 A; S/T/U/V=58-180.
DR PDB; 1UPM; X-ray; 2.30 A; C/F/I/M/P/S/T/W=58-180.
DR PDB; 1UPP; X-ray; 2.30 A; I/J/K/L=58-180.
DR PDB; 1UZD; X-ray; 2.40 A; C/F/I/J/M/P/T/W=103-121.
DR PDBsum; 1AA1; -.
DR PDBsum; 1AUS; -.
DR PDBsum; 1IR1; -.
DR PDBsum; 1UPM; -.
DR PDBsum; 1UPP; -.
DR PDBsum; 1UZD; -.
DR AlphaFoldDB; Q43832; -.
DR SMR; Q43832; -.
DR IntAct; Q43832; 1.
DR MINT; Q43832; -.
DR PRIDE; Q43832; -.
DR EvolutionaryTrace; Q43832; -.
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; IPR024680; RuBisCO_ssu_N.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 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; SSF55239; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Photorespiration; Photosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 57..180
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031558"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:1IR1"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:1IR1"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1IR1"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1IR1"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:1IR1"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1IR1"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1IR1"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:1IR1"
SQ SEQUENCE 180 AA; 20326 MW; 651FF2F212CFD64A CRC64;
MASSVLSSAA VATVSRTPAQ ASMVAPFTGL KSTVGFPATK KNDDITSLAS NGGRVQCMKV
WPTQNMKRYE TLSYLPPLTT DQLARQVDYL LNNKWVPCLE FETDHGFVYR EHHNSPGYYD
GRYWTMWKLP MFGCTDPAQV LNELEECKKE YPNAFIRIIG FDSNRQVQCV SFIAYKPAGY
