RBL_EUGLO
ID RBL_EUGLO Reviewed; 475 AA.
AC P26490;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
GN Name=rbcL;
OS Euglena longa (Euglenophycean alga) (Astasia longa).
OG Plastid; Non-photosynthetic plastid.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DETECTION OF PROTEIN.
RC STRAIN=CCAP 1204-17a;
RX PubMed=2102860; DOI=10.1007/bf00016515;
RA Siemeister G., Hachtel W.;
RT "Structure and expression of a gene encoding the large subunit of ribulose-
RT 1,5-bisphosphate carboxylase (rbcL) in the colourless euglenoid flagellate
RT Astasia longa.";
RL Plant Mol. Biol. 14:825-833(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1204-17a;
RX PubMed=11212895; DOI=10.1078/s1434-4610(04)70033-4;
RA Gockel G., Hachtel W.;
RT "Complete gene map of the plastid genome of the nonphotosynthetic euglenoid
RT flagellate Astasia longa.";
RL Protist 151:347-351(2000).
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 disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid.
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:0000250}.
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}.
CC -!- CAUTION: This organism being non-photosynthetic, the role of this
CC protein is uncertain. {ECO:0000305}.
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DR EMBL; AJ294725; CAC24574.1; -; Genomic_DNA.
DR PIR; S11855; RKITL.
DR RefSeq; NP_074963.1; NC_002652.1.
DR AlphaFoldDB; P26490; -.
DR SMR; P26490; -.
DR GeneID; 802514; -.
DR GO; GO:0009536; C:plastid; 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:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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; Disulfide bond; Lyase; Magnesium;
KW Metal-binding; Methylation; Monooxygenase; Oxidoreductase;
KW Photorespiration; Plastid.
FT CHAIN 1..475
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062366"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 52825 MW; 20CCBF03CFE3D9EF CRC64;
MPAQTESKTT TEFKAGVKDY KITYYTPDYK VSDTDVLAAF RMTPQTGVTP EECGAAVAAE
SSTGTWTTVW TDGLTQLDRY KGRCYDIEPV YGECDQYIAY IAYPIELFEE GSVTNLLTSI
VGNVFGFKAL RALRLEDLRI PACYLKSFWG PPHGIEVERD KLCKYGRGLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVTSQA FMRWRDRFLF CAEAIYKAQK ESGEVKGHYL
NVTAGNCEEM YKRADYAVKL GVPIIMHDFL TGGFTANTSL SNYCRNNGLL LHIHRAMHAV
IDRQRNHGIH FRVLAKTLRM SGGDHLHSGT VVGKLEGDRA GTYGFINLMR QNLIYRDRAC
GVYFAQDWCG LASLMPVASG GIHVWHMPAL LDIFGDDTCF QFGGGTLGHP WGNASGAVAN
RVALEACTQA RNEGKSLVKY GADIIREACK YSRELAAACD VWKEVTFNFD TVDKL
