ID Q9GFX5_CHRAL Unreviewed; 459 AA.
AC Q9GFX5;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:BAB20785.1};
OS Chrysochromulina alifera (Plankton alga).
OG Plastid {ECO:0000313|EMBL:BAB20785.1}.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=35141 {ECO:0000313|EMBL:BAB20785.1};
RN [1] {ECO:0000313|EMBL:BAB20785.1}
RP NUCLEOTIDE SEQUENCE.
RA Fujiwara S., Tsuzuki M., Kawachi M., Minaka N., Inouye I.;
RT "Molecular phylogeny of the Haptophyta based on the rbcL gene and sequence
RT variation in the spacer region of RuBisCO operon.";
RL J. Phycol. 37:121-129(2001).
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};
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DR EMBL; AB043695; BAB20785.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GFX5; -.
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: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 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 4: Predicted;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
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 Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 1..118
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 130..436
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:BAB20785.1"
FT NON_TER 459
FT /evidence="ECO:0000313|EMBL:BAB20785.1"
SQ SEQUENCE 459 AA; 50508 MW; EB173E0BF59D578D CRC64;
DPDYVIKETD LLALFRCTPQ PGVDPVEAAA ALAGESSTAT WTVVWTDLLT ACDLYRAKAY
RVDPVPNASD TYFCYIAYDI DLFEEGSLAN LTASIIGNIF GFKAVKALRL EDMRFPYALL
KTFQGPATGL VVERERMDKF GRPLLGATVK PKLGLSGKNY GRVVFEGLKG GLDFLKDDEN
INSQPFMRYR ERFLYSMEGV NHASSMSGEV KGHYLNTTGA TMEDMYERAD FAAELGSIVV
MIDLVIGYTA IQSMAIWSRK NDVILHLHRA GNSTYSRQKN HGMNFRVICK WMRMAGVDHI
HAGTVVGKLE GDPLMIKGFY NTLLDTKTDI NLPEGLFFAQ DWASLRKCVP VASGGIHCGQ
MHQLIDYLGE DCVMQFGGGT IGHPDGIQAG ATANRVALEC MVLARNEGRD YTNEGPQILR
DAAKSCGPLQ TALDLWKDIT FNYASTDTAD FATTATANV
//
