ID RBL_BETNI Reviewed; 466 AA.
AC P28384;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-APR-2013, entry version 72.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
DE Flags: Fragment;
GN Name=rbcL;
OS Betula nigra (River birch).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Fagales; Betulaceae; Betula.
OX NCBI_TaxID=3508;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1523408; DOI=10.1126/science.1523408;
RA Albert V.A., Williams S.E., Chase M.W.;
RT "Carnivorous plants: phylogeny and structural evolution.";
RL Science 257:1491-1495(1992).
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; L01889; AAA84040.2; -; Genomic_DNA.
DR EMBL; L12634; AAA84041.2; -; Genomic_DNA.
DR ProteinModelPortal; P28384; -.
DR SMR; P28384; 1-466.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:EC.
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 Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond;
KW Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
FT CHAIN <1 466 Ribulose bisphosphate carboxylase large
FT chain.
FT /FTId=PRO_0000062376.
FT ACT_SITE 166 166 Proton acceptor (By similarity).
FT ACT_SITE 285 285 Proton acceptor (By similarity).
FT METAL 192 192 Magnesium; via carbamate group (By
FT similarity).
FT METAL 194 194 Magnesium (By similarity).
FT METAL 195 195 Magnesium (By similarity).
FT BINDING 114 114 Substrate; in homodimeric partner (By
FT similarity).
FT BINDING 164 164 Substrate (By similarity).
FT BINDING 168 168 Substrate (By similarity).
FT BINDING 286 286 Substrate (By similarity).
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 370 370 Substrate (By similarity).
FT SITE 325 325 Transition state stabilizer (By
FT similarity).
FT MOD_RES 5 5 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 192 192 N6-carboxylysine (By similarity).
FT DISULFID 238 238 Interchain; in linked form (By
FT similarity).
FT NON_TER 1 1
SQ SEQUENCE 466 AA; 51699 MW; 35CD5130659291F1 CRC64;
SVAFKAGVKE YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV
WTDGLTSLDR YKGRCYHIEP VAGEESQFIA YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA
LRALRLEDLR IPPAYSKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEAIYKAQ AETGEIKGHY LNATAGTCEE
MMKRAIFARE LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM
HFRVLAKALR MSGGDHIHAG TVVGKLEGER EITLGFVDLL RDDYIEKDRS RGIYFTQDWV
SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ
ARNEGRDLAR EGNEIIREAA KWSPELAAAC EVWKEIKFEF PAMDTL
//
