RBL_NEOHI
ID RBL_NEOHI Reviewed; 488 AA.
AC Q760R5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
GN Name=rbcL;
OS Neoporphyra haitanensis (Red seaweed) (Porphyra haitanensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neoporphyra.
OX NCBI_TaxID=1262161;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Thallus;
RA Kito H., Kunimoto M., Mizukami Y., Murase N., Kuroki T., Taruta M.,
RA Levine I.;
RT "Species determination utilizing Porphyra (Rhodophyta) plastid DNA RuBisCo
RT sequences.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel' (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000305}.
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DR EMBL; AB118585; BAC84937.1; -; Genomic_DNA.
DR RefSeq; YP_007947755.1; NC_021189.1.
DR AlphaFoldDB; Q760R5; -.
DR SMR; Q760R5; -.
DR GeneID; 15525243; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 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; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid.
FT CHAIN 1..488
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000277257"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 337
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 54030 MW; 9081549622D2D44E CRC64;
MSQSVESRTR IKSERYESGV IPYAKMGYWD ADYVIKETDV LALFRITPQP GVDPIEASAA
IAGESSTATW TVVWTDLLTA CDLYRAKAYR VDPVPNVADQ YFAYIAYDID LFEEGSIANL
TASIIGNVFG FKAVKALRLE DMRMPVAYLK TFQGPATGLI VERERMDKFG RPFLGATVKP
KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWKE RFLYSMEGVN KASAAAGEIK
GHYLNVTAAT MEDMYERAEF SKEVGSIICM IDLVIGYTAI QTMAIWARKH DMILHLHRAG
NSTYSRQKNH GMNFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMIKGFYN TLLESETDIN
LPQGLFFAQN WASLRKVVPV ASGGIHAGQM HQLLDYLGDD VVLQFGGGTI GHPDGIQAGA
TANRVALESM VMARNEGRNY VAEGPQILRD AAKTCGPLQT ALDLWKDISF NYTSTDTADF
VETPTANI
