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Database: UniProt
Entry: B7FCF4_9ASPA
LinkDB: B7FCF4_9ASPA
Original site: B7FCF4_9ASPA 
ID   B7FCF4_9ASPA            Unreviewed;       438 AA.
AC   B7FCF4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:CAO85660.1};
OS   Cranichis sylvatica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Orchidoideae; Cranichideae; Cranichidinae; Cranichis.
OX   NCBI_TaxID=415399 {ECO:0000313|EMBL:CAO85660.1};
RN   [1] {ECO:0000313|EMBL:CAO85660.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Salazar G.A., Chase M.W., Cabrera L.I.;
RT   "Phylogenetics of Cranchidinae and Prescottiinae (Orchidaceae,
RT   Cranichideae) from plastid and nuclear DNA sequences.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00001067};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000256|ARBA:ARBA00000537};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR   EMBL; AM778150; CAO85660.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7FCF4; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020888; RuBisCO_lsuI.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDG01052; RuBisCO; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT   DOMAIN          11..131
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          141..427
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAO85660.1"
FT   NON_TER         438
FT                   /evidence="ECO:0000313|EMBL:CAO85660.1"
SQ   SEQUENCE   438 AA;  48623 MW;  55627D1CC9280871 CRC64;
     KAGVKDYKLT YYTPDYETKD TDILAAFRVT PQPGVPPEEA GAAVAAESST GTWTTVWTDG
     LTSLDRYKGR CYDIEAVVGE ENQYIAYVAY PLDLFEEGSV TNMFTSIVGN VFGFKALRAL
     RLEDLRIPTS YSKTFQGPPH GIQVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL
     RGGLDFTKDD ENVNSQPFMR WRDRFLFCAE SLYKAQAETG EIKGHYLNAT AGTCEEMMKR
     AVFARELGVP IVMHDYLTGG FTANTSLAHY CRDNGLLLHI HRAMHAVIDR QKNHGMHFRV
     LAKALRMSGG DHIHAGTVVG KLEGEREMTL GFVDLLRDDF IEKDRSRGIF FTQDWVSMPG
     VLPVASGGIH VWHMPALTEI FGDDSVLQFG GGTLGHPWGN APGAVANRVA LEACVQARNE
     GRDLAREGND IIREASKW
//
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