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RBS3_LEMGI
ID   RBS3_LEMGI              Reviewed;         177 AA.
AC   P19309;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit SSU40A {ECO:0000303|PubMed:2103442};
DE   Flags: Precursor;
GN   Name=RBCS3 {ECO:0000255|HAMAP-Rule:MF_00860};
GN   Synonyms=SSU40A {ECO:0000303|PubMed:2103442};
OS   Lemna gibba (Swollen duckweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Lemnoideae; Lemna.
OX   NCBI_TaxID=4470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=2103442; DOI=10.1007/bf00017723;
RA   Silverthorne J., Wimpee C.F., Yamada T., Rolfe S.A., Tobin E.M.;
RT   "Differential expression of individual genes encoding the small subunit of
RT   ribulose-1,5-bisphosphate carboxylase in Lemna gibba.";
RL   Plant Mol. Biol. 15:49-58(1990).
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   -!- INDUCTION: Accumulates to low levels when grown under continuous white
CC       light. {ECO:0000269|PubMed:2103442}.
CC   -!- MISCELLANEOUS: This protein is coded by one member of a small multigene
CC       family.
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; X17233; CAA35102.1; -; Genomic_DNA.
DR   PIR; S11681; RKDWS4.
DR   AlphaFoldDB; P19309; -.
DR   SMR; P19309; -.
DR   PRIDE; P19309; -.
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   2: Evidence at transcript level;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW   Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           57..177
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031514"
SQ   SEQUENCE   177 AA;  19802 MW;  B30738631E1581A7 CRC64;
     MASSMMASTA AAVARAGPAQ SSMVPFNACR SSVPFPATRK ANNNLSTLPG NGGRVSCMQV
     WPPEGLKKFE TLSYLPPLSV EDLAKEVDYL LRNDWVPCIE FSKEGFVYRE NHASPGYYDG
     RYWTMWKLPM FGCTDASQVI AEVEEAKKAY PEYFVRIIGF DNKRQVQCIS FIAYKPT
 
 
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