ID D1J7D7_ECTSI Unreviewed; 139 AA.
AC D1J7D7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
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:CAV31321.1};
GN Synonyms=RBCS {ECO:0000256|HAMAP-Rule:MF_00860};
GN ORFNames=Es_cpDNA_178 {ECO:0000313|EMBL:CAV31321.1}, Esil_029
GN {ECO:0000313|EMBL:QIE12375.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OG Plastid {ECO:0000313|EMBL:CAV31321.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CAV31321.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAV31321.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=19835607; DOI=10.1186/1471-2148-9-253;
RA Le Corguille G., Pearson G., Valente M., Viegas C., Gschloessl B.,
RA Corre E., Bailly X., Peters A.F., Jubin C., Vacherie B., Cock J.M.,
RA Leblanc C.;
RT "Plastid genomes of two brown algae, Ectocarpus siliculosus and Fucus
RT vesiculosus: further insights on the evolution of red-algal derived
RT plastids.";
RL BMC Evol. Biol. 9:253-253(2009).
RN [3] {ECO:0000313|EMBL:QIE12375.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=32029782;
RA Choi J.W., Graf L., Peters A.F., Cock J.M., Nishitsuji K., Arimoto A.,
RA Shoguchi E., Nagasato C., Choi C.G., Yoon H.S.;
RT "Organelle inheritance and genome architecture variation in isogamous brown
RT algae.";
RL Sci. Rep. 10:0-2048(2020).
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_00859}.
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; FP102343; CAT18877.1; -; Genomic_DNA.
DR EMBL; FP102296; CAV31321.1; -; Genomic_DNA.
DR EMBL; MN181444; QIE12375.1; -; Genomic_DNA.
DR RefSeq; YP_003289290.1; NC_013498.1.
DR AlphaFoldDB; D1J7D7; -.
DR STRING; 2880.D1J7D7; -.
DR GeneID; 8594836; -.
DR InParanoid; D1J7D7; -.
DR Proteomes; UP000002630; 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 3: Inferred from homology;
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:CAV31321.1};
KW Lyase {ECO:0000313|EMBL:CAV31321.1};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW Rule:MF_00860};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00860};
KW Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000313|EMBL:CAV31321.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 4..103
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
SQ SEQUENCE 139 AA; 15899 MW; 2BEBD78DCCB8628C CRC64;
MRVTQGCFSF LPDLSDDQIK QQVAYAMSKG WAVSVEWTDD PHPRNSYWEL WGLPLFDVKD
PAAVMYELAE CRKVNPEGYI KINAFDASIG TESCVMSFIV QRPITEPGFY LERNEVQGRN
IQYTISSYAV QARPSGDRY
//
