RBL2_HETTR
ID RBL2_HETTR Reviewed; 740 AA.
AC Q5ENN5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ribulose bisphosphate carboxylase, chloroplastic;
DE Short=RuBisCO;
DE EC=4.1.1.39;
DE Flags: Precursor;
GN Name=rbcL;
OS Heterocapsa triquetra (Dinoflagellate) (Glenodinium triquetrum).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Peridiniales; Heterocapsaceae;
OC Heterocapsa.
OX NCBI_TaxID=66468;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CCMP449;
RX PubMed=15843030; DOI=10.1016/j.jmb.2005.03.030;
RA Patron N.J., Waller R.F., Archibald J.M., Keeling P.J.;
RT "Complex protein targeting to dinoflagellate plastids.";
RL J. Mol. Biol. 348:1015-1024(2005).
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. Both reactions occur simultaneously and in competition at
CC the same active site (By 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: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305}.
CC Note=In this organism the plastid is the result of a secondary
CC endosymbiosis event, and thus is found within the endomembrane system,
CC necessitating a complex targeting process.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In contrast to form I
CC RuBisCO, the form II RuBisCO are composed solely of large subunits (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is suggested in PubMed:15843030 to be first
CC cotranslationally imported into the ER up to the stop-transfer signal,
CC so that the N-terminal region of the transit peptide is in the lumen of
CC the ER while the rest of the protein remains in the cytoplasm.
CC Maintaining this topology, proteins are directed to the Golgi and
CC sorted into vesicles that will fuse with the outermost plastid
CC membrane, exposing the transit peptide to the Toc/Tic apparatus, which
CC draws the entire protein across the remaining membranes.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Note that unlike other eukaryotes, peridinin-containing
CC dinoflagellates have a nuclear-encoded chloroplast-targeted form II
CC RuBisCO. {ECO:0000305}.
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DR EMBL; AY826897; AAW79358.1; -; mRNA.
DR AlphaFoldDB; Q5ENN5; -.
DR SMR; Q5ENN5; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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 CDD; cd08211; RuBisCO_large_II; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 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; IPR020871; RuBisCO_lsuII.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 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; Lyase; Magnesium;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..740
FT /note="Ribulose bisphosphate carboxylase, chloroplastic"
FT /id="PRO_0000042970"
FT TRANSMEM 56..76
FT /note="Helical; Note=Stop-transfer"
FT /evidence="ECO:0000255"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 431
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 293
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
SQ SEQUENCE 740 AA; 79148 MW; E13467039029BA77 CRC64;
MPSSSFTTGL ALGAGALVGA NAFVAPTAKT TNLRAPTQEA SLQVAASQQT EQPAPSTSAL
PWAFGAGACL ALAAGGQRKQ RSAIAQGRAT VLPTASPVVR RALDQSSRYA DLSLSEEQLI
ANGKHVLVSY IMKPKAGYDY LATAAHFAAE SSTGTNVNVC TTDDFTKSVD ALVYYIDPEN
EECKIAYPNL LFDRNIIDGR AMMCSVLTLT IGNNQGMGDV EYGKIYDIYF PPSYLRLFDG
PSCNIIDMWR ILGRGTTDGG LVVGTIIKPK LGLQPKPFGE ACYAFWQGGD FIKNDEPQGN
QPFCQMNEVI PEVVKAMRAA IKETGVAKLF SANITADDPA EMIARGKYVL AQFGPLSENC
AFLVDGYVAG GTAVTVARRN FPKQFLHYHR AGHGSVTSPQ TQRGYTAFVH TKLSRVQGAS
GIHVGTMSFG KMEGDASDKN IAFMLQDDAA DGPYYHQTWE GMAETTPIIS GGMNALRLPA
FFENLGHSNV ILTAGGGAFG HKDGPKQGAT SCRQGEEAWK LWKAGVYGSV SLSDGVIEYA
KTHEEIKGAF LTFQKDADQI YPGWKEKLGY TGESSVQAAS FDWKKKAAAA AFAGSSTQAR
TVGVQMRHGY DDVATNTFYY DKRLESFGQQ EFFNQVGYLP DGTPMNTAGN LTNHPETIGP
DPHINGSELP QAVFVNSIGY LPDGTAMNQA GNAVNHPETM GPDLHMAGSP LPPPLKGYLN
DIGYLSDGTP MATAGNLSNH
