RBL_EUGGR
ID RBL_EUGGR Reviewed; 475 AA.
AC P00878; P48071;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Euglena gracilis.
OG Plastid; Chloroplast.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999148; DOI=10.1016/s0021-9258(17)36214-2;
RA Gingrich J.C., Hallick R.B.;
RT "The Euglena gracilis chloroplast ribulose-1,5-bisphosphate carboxylase
RT gene. I. Complete DNA sequence and analysis of the nine intervening
RT sequences.";
RL J. Biol. Chem. 260:16156-16161(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3934171; DOI=10.1016/s0021-9258(17)36215-4;
RA Gingrich J.C., Hallick R.B.;
RT "The Euglena gracilis chloroplast ribulose-1,5-bisphosphate carboxylase
RT gene. II. The spliced mRNA and its product.";
RL J. Biol. Chem. 260:16162-16168(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA Spielmann A., Stutz E.;
RT "Complete sequence of Euglena gracilis chloroplast DNA.";
RL Nucleic Acids Res. 21:3537-3544(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-204.
RX PubMed=6319030; DOI=10.1016/0092-8674(84)90247-2;
RA Koller B., Gingrich J.C., Stiegler G.L., Farley M.A., Delius H.,
RA Hallick R.B.;
RT "Nine introns with conserved boundary sequences in the Euglena gracilis
RT chloroplast ribulose-1,5-bisphosphate carboxylase gene.";
RL Cell 36:545-553(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-455.
RC STRAIN=UTEX 364;
RX PubMed=8532514; DOI=10.1093/nar/23.23.4745;
RA Thompson M.D., Copertino D.W., Thompson E., Favreau M.R., Hallick R.B.;
RT "Evidence for the late origin of introns in chloroplast genes from an
RT evolutionary analysis of the genus Euglena.";
RL Nucleic Acids Res. 23:4745-4752(1995).
RN [6]
RP ERRATUM OF PUBMED:8532514, AND SHOWS THAT UTEX 364 IS FROM E.GRACILIS AND
RP NOT E.MUTABILIS.
RA Thompson M.D., Copertino D.W., Thompson E., Favreau M.R., Hallick R.B.;
RL Nucleic Acids Res. 24:1792-1792(1996).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338};
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:0000255|HAMAP-Rule:MF_01338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}.
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'.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; M15391; AAA84221.1; -; Genomic_DNA.
DR EMBL; M12109; AAA84453.1; -; Genomic_DNA.
DR EMBL; X70810; CAA50123.1; -; Genomic_DNA.
DR EMBL; U21006; AAA91979.1; -; mRNA.
DR PIR; A24556; RKEGL.
DR PIR; S66168; S66168.
DR RefSeq; NP_041936.1; NC_001603.2.
DR AlphaFoldDB; P00878; -.
DR SMR; P00878; -.
DR GeneID; 807506; -.
DR SABIO-RK; P00878; -.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid.
FT CHAIN 1..475
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062467"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 103..107
FT /note="YPIDL -> SLLIF (in Ref. 4; AAA84221)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> S (in Ref. 5; AAA91979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52609 MW; 558578D7A3E2205B CRC64;
MSPQTETKTG AGFKAGVKDY RLTYYTPDYQ VSETDILAAF RMTPQPGVPA EECGAAVAAE
SSTGTWTTVW TDGLTQLDRY KGRCYDLEPV PGESNQYIAY VAYPIDLFEE GSVTNLLTSI
VGNVFGFKAL RALRLEDLRI PPAYSKTFWG PPHGIQVERD RLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQS FMRWRDRFLF CAEAIYKAQT ETGEVKGHYL
NATAGTCEEM YKRASFAAQI GVPIIMHDYL TGGFTANTSL AMYCRDNGLL LHIHRAMHAV
IDRQRNHGIH FRVLAKTLRM SGGDHLHSGT VVGKLEGERE VTLGFVDLMR DAYVEKDRSR
GIYFTQDWCG MGGTMPVASG GIHVWHMPAL TEIFGDDACL QFGGGTLGHP WGNAPGAAAN
RVASEACVQA RNEGRDLSRE GGDVIREACK WSPELAAACE VWKEIKFEFE TIDKL
