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Database: UniProt
Entry: A4QJU1
LinkDB: A4QJU1
Original site: A4QJU1 
ID   RBL_OLIPU               Reviewed;         479 AA.
AC   A4QJU1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   14-MAY-2014, entry version 38.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=rbcL;
OS   Olimarabidopsis pumila (Dwarf rocket) (Arabidopsis griffithiana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
OC   Alyssopsideae; Olimarabidopsis.
OX   NCBI_TaxID=74718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequence analysis of Arabidopsis pumila JS2 chloroplast DNA.";
RL   Submitted (MAR-2007) 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 in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC       disulfide-linked. The disulfide link is formed within the large
CC       subunit homodimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with
CC       oxidative stress and protein turnover (By similarity).
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In form I
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel" (By similarity).
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily.
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DR   EMBL; AP009368; BAF49947.1; -; Genomic_DNA.
DR   RefSeq; YP_001123123.1; NC_009267.1.
DR   ProteinModelPortal; A4QJU1; -.
DR   SMR; A4QJU1; 9-472.
DR   GeneID; 4962430; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR020888; RuBisCO_lsu.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR017444; RuBisCO_lsu_N.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond;
KW   Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Phosphoprotein; Photorespiration; Photosynthesis; Plastid.
FT   PROPEP        1      2       By similarity.
FT                                /FTId=PRO_0000300005.
FT   CHAIN         3    479       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000300006.
FT   ACT_SITE    175    175       Proton acceptor (By similarity).
FT   ACT_SITE    294    294       Proton acceptor (By similarity).
FT   METAL       201    201       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       203    203       Magnesium (By similarity).
FT   METAL       204    204       Magnesium (By similarity).
FT   BINDING     123    123       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     173    173       Substrate (By similarity).
FT   BINDING     177    177       Substrate (By similarity).
FT   BINDING     295    295       Substrate (By similarity).
FT   BINDING     327    327       Substrate (By similarity).
FT   BINDING     379    379       Substrate (By similarity).
FT   SITE        334    334       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     201    201       N6-carboxylysine (By similarity).
FT   MOD_RES     330    330       Phosphothreonine (By similarity).
FT   DISULFID    247    247       Interchain; in linked form (By
FT                                similarity).
SQ   SEQUENCE   479 AA;  52969 MW;  6D70AB57CD787166 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEETQFIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL AALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL SHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRL SGGDHVHAGT VVGKLEGDRE STLGFVDLLR DDYIEKDRSR
     GIFFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLAVE GNEIIREACK WSPELAAACE VWKEIRFNFP TVDTLDDQA
//
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