ID   O98950_9RHOD            Unreviewed;       138 AA.
AC   O98950;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00859, ECO:0000256|HAMAP-Rule:MF_00860};
DE   Includes:
DE     RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE              Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE   Includes:
DE     RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860};
GN   Name=rbcS {ECO:0000256|HAMAP-Rule:MF_00859,
GN   ECO:0000313|EMBL:BAA75797.1};
GN   Synonyms=RBCS {ECO:0000256|HAMAP-Rule:MF_00860};
GN   ORFNames=GpartN1_CHLp155 {ECO:0000313|EMBL:BDE17661.1};
OS   Galdieria partita.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAA75797.1}.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=83374 {ECO:0000313|EMBL:BAA75797.1};
RN   [1] {ECO:0000313|EMBL:BAA75797.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tomizawa K.;
RT   "Structure and function study of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase of the red algae, Galdieria partita Tokara.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:1BWV}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-138.
RX   PubMed=10336462; DOI=10.1074/jbc.274.22.15655;
RA   Sugawara H., Yamamoto H., Shibata N., Inoue T., Okada S., Miyake C.,
RA   Yokota A., Kai Y.;
RT   "Crystal structure of carboxylase reaction-oriented ribulose 1, 5-
RT   bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria
RT   partita.";
RL   J. Biol. Chem. 274:15655-15661(1999).
RN   [3] {ECO:0007829|PDB:1IWA}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RX   PubMed=12220629; DOI=10.1016/s0014-5793(02)03148-4;
RA   Okano Y., Mizohata E., Xie Y., Matsumura H., Sugawara H., Inoue T.,
RA   Yokota A., Kai Y.;
RT   "X-ray structure of Galdieria Rubisco complexed with one sulfate ion per
RT   active site.";
RL   FEBS Lett. 527:33-36(2002).
RN   [4] {ECO:0000313|EMBL:BDE17661.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 102759 {ECO:0000313|EMBL:BDE17661.1};
RA   Hirooka S., Itabashi T., Ichinose T.M., Onuma R., Fujiwara T.,
RA   Yamashita S., Jong L.W., Tomita R., Iwane A.H., Miyagishima S.Y.;
RT   "Life cycle and functional genomics of the unicellular red alga Galdieria
RT   for elucidating algal and plant evolution and industrial use.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:e2210665119-e2210665119(2022).
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 in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site. Although the
CC       small subunit is not catalytic it is essential for maximal activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
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   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|ARBA:ARBA00038826, ECO:0000256|HAMAP-Rule:MF_00859}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_00859}.
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_00859}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
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DR   EMBL; AB018008; BAA75797.1; -; Genomic_DNA.
DR   EMBL; AP025529; BDE17661.1; -; Genomic_DNA.
DR   PDB; 1BWV; X-ray; 2.40 A; S/U/W/Y=1-138.
DR   PDB; 1IWA; X-ray; 2.60 A; B/D/F/H/J/L/N/P=1-138.
DR   PDBsum; 1BWV; -.
DR   PDBsum; 1IWA; -.
DR   AlphaFoldDB; O98950; -.
DR   SMR; O98950; -.
DR   EvolutionaryTrace; O98950; -.
DR   Proteomes; UP001061958; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; 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:SF23; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1BWV, ECO:0007829|PDB:1IWA};
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Chloroplast {ECO:0000256|HAMAP-Rule:MF_00859, ECO:0000313|EMBL:BAA75797.1};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000313|EMBL:BAA75797.1}.
FT   DOMAIN          4..103
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   138 AA;  16189 MW;  6A98CBB2BE0620BE CRC64;
     MRITQGTFSF LPDLTDEQIK KQIDYMISKK LAIGIEYTND IHPRNAYWEI WGLPLFDVTD
     PAAVLFEINA CRKARSNFYI KVVGFSSVRG IESTIISFIV NRPKHEPGFN LMRQEDKSRS
     IKYTIHSYES YKPEDERY
//