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 03-APR-2013, entry version 34.
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; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC 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 ProtClustDB; CHL00040; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA: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; RuBisCO_large; 1.
DR SUPFAM; SSF54966; RuBisCO_large; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 3: Inferred from homology;
KW Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation;
KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis;
KW 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 3 3 N-acetylproline (By similarity).
FT MOD_RES 14 14 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 201 201 N6-carboxylysine (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
//
