ID B6ZGV7_9FLOR Unreviewed; 410 AA.
AC B6ZGV7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 03-MAY-2023, entry version 47.
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;
GN Name=rbcL {ECO:0000313|EMBL:BAH02510.1};
OS Peyssonnelia japonica.
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAH02510.1}.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae;
OC Peyssonneliales; Peyssonneliaceae; Peyssonnelia.
OX NCBI_TaxID=339595 {ECO:0000313|EMBL:BAH02510.1};
RN [1] {ECO:0000313|EMBL:BAH02510.1}
RP NUCLEOTIDE SEQUENCE.
RA Kato A., Guimaraes S.M.P.B., Kawai H., Masuda M.;
RT "Characterization of the crustose red alga Peyssonnelia japonica
RT (Rhodophyta, Gigartinales) and its taxonomic relationship with Peyssonnelia
RT boudouresquei based on morphological and molecular data.";
RL Phycol. Res. 57:74-86(2009).
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 ECO:0000256|RuleBase:RU000302};
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 ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
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:RU000302}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU000302}.
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DR EMBL; AB325817; BAH02510.1; -; Genomic_DNA.
DR EMBL; AB325820; BAH02513.1; -; Genomic_DNA.
DR EMBL; AB325821; BAH02514.1; -; Genomic_DNA.
DR EMBL; AB325822; BAH02515.1; -; Genomic_DNA.
DR AlphaFoldDB; B6ZGV7; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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 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 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 ECO:0000256|RuleBase:RU000302};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU000302};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:BAH02510.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000302};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000302};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000302};
KW Photorespiration {ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:BAH02510.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 228..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..112
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 122..406
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:BAH02510.1"
FT NON_TER 410
FT /evidence="ECO:0000313|EMBL:BAH02510.1"
SQ SEQUENCE 410 AA; 45272 MW; 1AE546BA964F414F CRC64;
DTDVLALFRV SPQPGVDPVE ASAAVAGESS TATWTVVWTD LLTACDLYRA KAYKVDAVPN
TTDQYFAYIA YDIDLFEEGS IANLTASIIG NVFGFKAVKA LRLEDMRIPV AYLKTFQGPA
TGIVVERERM DKFGRPFLGA TVKPKLGLSG KNYGRVVYEG LKGGLDFLKD DENINSQPFM
RWKERFLYSM EAVNRSIAST GEVKGHYMNV TAATMEDMYE RAEFAKQLGT VIIMIDLVIG
YTAIQTMAIW ARKNDMILHL HRAGNSTYSR QKIHGMNFRV ICKWMRMAGV DHIHAGTVVG
KLEGDPVMIK GFYNTLLLPY LDVNLGQGIF FEQDWASLRK VTPVASGGIH CGQMHQLLDY
LGEDVVLQFG GGTIGHPDGI QAGATANRVA LESMLIARNE GRDYVAEGPQ
//
