ID A9NZM2_PICSI Unreviewed; 159 AA.
AC A9NZM2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00860};
GN Name=RBCS {ECO:0000256|HAMAP-Rule:MF_00860};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ABK26083.1};
RN [1] {ECO:0000313|EMBL:ABK26083.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Green portion of the leader tissue
RC {ECO:0000313|EMBL:ABK26083.1};
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
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 ECO:0000256|RuleBase:RU003627}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|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:0000256|HAMAP-Rule:MF_00860}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}.
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DR EMBL; EF086827; ABK26083.1; -; mRNA.
DR AlphaFoldDB; A9NZM2; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; 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:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 2; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE 2: Evidence at transcript level;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW Rule:MF_00860};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00860}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_00860};
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:0000256|RuleBase:RU003627};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..159
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002741850"
FT DOMAIN 48..156
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
SQ SEQUENCE 159 AA; 17998 MW; 409FD82EC017DB71 CRC64;
MASSIMALSS TAAVAAVAAP PKTSNGNGSS NGGRVRCMQV WPPYNNPKFE TLSYLPRLTQ
EQLLKEVEYL LRNKWVPCLE FDEDGIIKRK YGSTPGYYDG RYWVMWKLPM FGCTEASQVL
NEVNECAKAY PKAFIRVIGF DNVRQVQCIS FIVHKPEYN
//
