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RBS2_SOYBN
ID   RBS2_SOYBN              Reviewed;         178 AA.
AC   P12468;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 112.
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   AltName: Full=Ribulose bisphosphate carboxylase small chain 4, chloroplastic;
DE            Short=RuBisCO small subunit 4;
DE   Flags: Precursor;
GN   Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860};
GN   Synonyms=RBCS-4, SRS4 {ECO:0000303|PubMed:24302473};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=24302473; AGRICOLA=IND87019920; DOI=10.1007/BF00020329;
RA   Grandbastien M.-A., Berry-Lowe S., Shirley B.W., Meagher R.B.;
RT   "Two soybean ribulose-1,5-bisphosphate carboxylase small subunit genes
RT   share extensive homology even in distant flanking sequences.";
RL   Plant Mol. Biol. 7:451-465(1986).
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   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
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}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR   EMBL; M16889; AAA34008.1; -; Genomic_DNA.
DR   PIR; A30837; RKSYS4.
DR   AlphaFoldDB; P12468; -.
DR   SMR; P12468; -.
DR   PRIDE; P12468; -.
DR   InParanoid; P12468; -.
DR   Proteomes; UP000008827; Unplaced.
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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           55..178
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031557"
SQ   SEQUENCE   178 AA;  20017 MW;  1BE80EE9B625F6B4 CRC64;
     MASSMISSPA VTTVNRAGAG MVAPFTGLKS MAGLPTRKTN NDITSIASNG GRVQCMQVWP
     PVGKKKFETL SYLPDLDDAQ LAKEVEYLLR KGWIPCLEFE LEHGFVYREH NRSLGYYDGR
     YWTMWKLPMF GCTDASQVLK ELQEAKTAYP NGFIRIIGFD NVRQVQCISF IAYKPPSF
 
 
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