ID   RBL_MAGLA               Reviewed;         253 AA.
AC   P30828;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-NOV-2008, entry version 55.
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   Magnolia latahensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; magnoliids; Magnoliales; Magnoliaceae;
OC   Magnolia.
OX   NCBI_TaxID=3409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90220868; PubMed=2325772; DOI=10.1038/344656a0;
RA   Golenberg E.M., Giannasi D.E., Clegg M.T., Smiley C.J., Durbin M.,
RA   Henderson D., Zurawski G.;
RT   "Chloroplast DNA sequence from a miocene Magnolia species.";
RL   Nature 344:656-658(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 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.
CC   -!- CAUTION: This sequence originates from a miocene fossil leaf
CC       sample.
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DR   EMBL; X54344; CAA38232.1; -; Genomic_DNA.
DR   SMR; P30828; 1-253.
DR   GO; GO:0009573; C:chloroplast ribulose bisphosphate carboxyla...; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; 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   HAMAP; MF_01338; -; 1.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR017444; RuBisCO_lsu_N.
DR   Gene3D; G3DSA:3.20.20.110; RuBisCO_large; 1.
DR   Gene3D; G3DSA:3.30.70.150; RuBisCO_large; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Extinct organism protein; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis;
KW   Plastid.
FT   CHAIN        <1   >253       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062529.
FT   ACT_SITE     87     87       Proton acceptor (By similarity).
FT   ACT_SITE    206    206       Proton acceptor (By similarity).
FT   METAL       113    113       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       115    115       Magnesium (By similarity).
FT   METAL       116    116       Magnesium (By similarity).
FT   BINDING      35     35       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING      85     85       Substrate (By similarity).
FT   BINDING      89     89       Substrate (By similarity).
FT   BINDING     207    207       Substrate (By similarity).
FT   BINDING     239    239       Substrate (By similarity).
FT   SITE        246    246       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     113    113       N6-carboxylysine (By similarity).
FT   DISULFID    159    159       Interchain; in linked form (By
FT                                similarity).
FT   NON_TER       1      1
FT   NON_TER     253    253
SQ   SEQUENCE   253 AA;  28360 MW;  F182B07840842950 CRC64;
     PVAGEENQYI AYVAYPLDLF EEGSVTNMFT SIVGNVFGFK ALRALRLEDL RIPTAYVKTF
     QGPPHGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS
     QPFMRWRDRF LFCAEALYKA QAETGEIKGH YLNATAGTCE EMMKRAIFAR ELGVPIVMHD
     YLTGGFTANT SLAHYCRDNG LLLHIHRAMH AVIDRQKNHG IHFRVLAKAL RMSGGDHIHS
     GTVVGKLEGE RDI
//