RBS7_ACEPE
ID RBS7_ACEPE Reviewed; 183 AA.
AC Q38693;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 7 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 7 {ECO:0000255|HAMAP-Rule:MF_00860};
DE AltName: Full=rbcS1;
DE Flags: Precursor;
GN Name=RBCS7 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-7;
OS Acetabularia peniculus (Green alga) (Polyphysa peniculus).
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Dasycladales; Polyphysaceae; Acetabularia.
OX NCBI_TaxID=35862;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Frank S., Menzel D.;
RT "Characterization of two genes for isoforms of the small subunit of
RT ribulose-1,5-bisphosphate carboxylase oxygenase (rbcS) from the marine
RT unicellular green alga Acetabularia cliftonii (Dasycladales).";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
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; Z28636; CAA82265.1; -; Genomic_DNA.
DR AlphaFoldDB; Q38693; -.
DR SMR; Q38693; -.
DR PRIDE; Q38693; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 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; Lyase; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 44..183
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 7"
FT /id="PRO_0000031453"
SQ SEQUENCE 183 AA; 20553 MW; 59C8075B96500696 CRC64;
MAAAMMNKTV VVGKESVKGG VAPKVAMSRG GFLNSGIMKK DRDMMVWQPF NNKMFETFSY
LPPLTDEQIS KQVDYILANS WTPCLEFAAS DQAYAGNENC IRMGPVASTY QDNRYWTMWK
LPMFGCTDGS QVLSDMQACT KAFPDAYIRL VCFDANRQVQ ICGFLVHRPP SATDYRLPAD
RQV