ID   Q95DI4_9MONI            Unreviewed;       415 AA.
AC   Q95DI4;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   01-OCT-2014, entry version 55.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
DE            EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302};
DE   Flags: Fragment {ECO:0000313|EMBL:BAB69795.1};
GN   Name=rbcL {ECO:0000313|EMBL:BAB69795.1};
OS   Stegnogramma gymnocarpa.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAB69795.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Moniliformopses; Polypodiidae; Polypodiales; eupolypods II;
OC   Thelypteridaceae; Stegnogramma.
OX   NCBI_TaxID=157681 {ECO:0000313|EMBL:BAB69795.1};
RN   [1] {ECO:0000313|EMBL:BAB69795.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kakugawa-Yatabe Y., Murakami N.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAB69795.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yatabe Y., Murakami M.;
RT   "Cryptic Species in Stegnogramma pozoi.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU000303}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU004228}.
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DR   EMBL; AB059745; BAB69795.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q95DI4; -.
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:UniProtKB-EC.
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   InterPro; IPR020878; RuBisCo_large_chain_AS.
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 {ECO:0000256|RuleBase:RU000302};
KW   Carbon dioxide fixation {ECO:0000256|RuleBase:RU000302};
KW   Chloroplast {ECO:0000256|RuleBase:RU000303,
KW   ECO:0000313|EMBL:BAB69795.1}; Lyase {ECO:0000256|RuleBase:RU000302};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000302};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|RuleBase:RU004237};
KW   Plastid {ECO:0000313|EMBL:BAB69795.1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:BAB69795.1}.
FT   NON_TER     415    415       {ECO:0000313|EMBL:BAB69795.1}.
SQ   SEQUENCE   415 AA;  46086 MW;  D354DBDA3FE04C8B CRC64;
     KDYRLTYYTP EYKTKDTDIL AAFRMTPQPG VPAEEAGAAV AAESSTGTWT TVWTDGLTSL
     DRYKGRCYDI EPVAGEENQY IAYVAYPLDL FEEGSVTNLF TSIVGNVFGF KALRALRLED
     LRIPPAYSKT FMGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL
     DFTKDDENVN SQPFMRWRDR FLFVAEALFK SQAETGEIKG HYLNATAGTC EEMLKRAVFA
     RELGAPIVMH DYLTGGFTAN TSLAFYCRDN GLLLHIHRAM HAVIDRQRNH GMHFRVLAKA
     LRMSGGDHIH AGTVVGKLEG EREVTLGFVD LLRDDYIEKD RSRGIYFTQD WVSMPGVFPV
     ASGGIHVWHM PALTEIFGDD SVLQFGGGTL GHPWGNAPGA VANRVALEAC VQARN
//