ID Q9ZWH3_9POAL Unreviewed; 165 AA.
AC Q9ZWH3;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|RuleBase:RU003627};
DE Short=RuBisCO small subunit {ECO:0000256|RuleBase:RU003627};
DE Flags: Fragment;
GN Name=rbcS {ECO:0000313|EMBL:BAA35154.1};
OS Aegilops sharonensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=58530 {ECO:0000313|EMBL:BAA35154.1};
RN [1] {ECO:0000313|EMBL:BAA35154.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10085553; DOI=10.1266/ggs.73.297;
RA Sasanuma T., Miyashita N.T.;
RT "Subfamily devergence in the multigene family of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase (rbcS) in Triticeae and its relatives.";
RL Genes Genet. Syst. 73:297-309(1998).
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|RuleBase:RU003627}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000256|RuleBase:RU003627}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000256|RuleBase:RU003627}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB020935; BAA35154.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZWH3; -.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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; IPR024680; RuBisCO_ssu_N.
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; PF12338; RbcS; 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 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU003627};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238,
KW ECO:0000256|RuleBase:RU003627};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU003627}; Plastid {ECO:0000256|RuleBase:RU003627};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 53..161
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA35154.1"
FT NON_TER 165
FT /evidence="ECO:0000313|EMBL:BAA35154.1"
SQ SEQUENCE 165 AA; 18531 MW; 736FFB1F619E5291 CRC64;
VMASSATTVA PFQGLKSTAG LPVSRRSSGS LGSVSNGGRI RCMQVWPIEG IKKFETLSYL
PPLSTEALLK QVDYLIRSKW VPCLEFSKVG FVFREHNSSP GYYDGRYWTM WKLPMFGCTD
ATQVLNEVEE VKKEYPDAYV RVIGFDNLRQ VQCVSFIAFR PPGCE
//
