RBL2_SYMSP
ID RBL2_SYMSP Reviewed; 1501 AA.
AC Q41406;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ribulose bisphosphate carboxylase;
DE Short=RuBisCO;
DE EC=4.1.1.39;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase 1;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase 2;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase 3;
DE Flags: Precursor; Fragment;
GN Name=rbcL; Synonyms=rbcA;
OS Symbiodinium sp. (Dinoflagellate).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21; 30-45;
RP 65-97; 146-160; 240-252; 330-348 AND 371-388.
RX PubMed=8721755; DOI=10.2307/3870331;
RA Rowan R., Whitney S.M., Fowler A., Yellowlees D.;
RT "Rubisco in marine symbiotic dinoflagellates: form II enzymes in eukaryotic
RT oxygenic phototrophs encoded by a nuclear multigene family.";
RL Plant Cell 8:539-553(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. 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 {ECO:0000305}. Note=In this
CC organism the plastid is the result of a secondary endosymbiosis event,
CC and thus is found within the endomembrane system, necessitating a
CC 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: Synthesized as an approximately 175 kDa polyprotein,
CC imported into chloroplasts and subsequently cleaved into 3 mature
CC RuBisCO proteins. All 3 RuBisCO copies are present in this protein.
CC -!- MISCELLANEOUS: This may be first cotranslationally imported into the ER
CC up to a stop-transfer signal, so that the N-terminal region of the
CC transit peptide is in the lumen of the ER while the rest of the protein
CC remains in the cytoplasm. Maintaining this topology, proteins are
CC directed to the Golgi and sorted into vesicles that will fuse with the
CC outermost plastid membrane, exposing the transit peptide to the Toc/Tic
CC apparatus, which draws the entire protein across the remaining
CC membranes (By similarity). {ECO:0000250}.
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; U43532; AAB17550.1; -; Genomic_DNA.
DR PIR; T29094; T29094.
DR AlphaFoldDB; Q41406; -.
DR SMR; Q41406; -.
DR BRENDA; 4.1.1.39; 7052.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 3.
DR Gene3D; 3.20.20.110; -; 3.
DR Gene3D; 3.30.70.150; -; 3.
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; 3.
DR Pfam; PF00016; RuBisCO_large; 3.
DR Pfam; PF02788; RuBisCO_large_N; 3.
DR SUPFAM; SSF51649; SSF51649; 3.
DR SUPFAM; SSF54966; SSF54966; 3.
DR PROSITE; PS00157; RUBISCO_LARGE; 3.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis; Plastid; Repeat.
FT CHAIN 1..485
FT /note="Ribulose bisphosphate carboxylase 1"
FT /id="PRO_0000042978"
FT PROPEP 486..508
FT /note="Linker"
FT /id="PRO_0000042979"
FT CHAIN 509..993
FT /note="Ribulose bisphosphate carboxylase 2"
FT /id="PRO_0000042980"
FT PROPEP 994..1016
FT /note="Linker"
FT /id="PRO_0000042981"
FT CHAIN 1017..1501
FT /note="Ribulose bisphosphate carboxylase 3"
FT /id="PRO_0000042982"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 674
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 795
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1303
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 701
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 796
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 876
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1127
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 1184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 837
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 1345
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT MOD_RES 699
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT MOD_RES 1207
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT CONFLICT 1
FT /note="L -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1
FT /note="L -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="W -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..249
FT /note="MS -> TD (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1501 AA; 164385 MW; C184A9F96F94B2A7 CRC64;
LDQSSRYADL SLDEDTLIRN GKHVLVAYIM KPKAGYDYLA TAAHFAAESS TGTNVNVCTT
DDFTKSVDAL VYYIDPDNEE MKIAYPTLLF DRNITDGRGM MCSFLTLAIG NNQGMGDVEY
GKIYDFYLPP AFLRLYDGPS VNVEDMWRIL GRGTTNGGLV VGTIIKPKLG LQPKPFGEAC
YSFWQGGDFI KNDEPQGNQV FCQMNECIPE VVKAMRACVK ETGSSKLFSA NITADDPEEM
IARGKYIMSQ FGPLSENCAF LVDGYVAGGT AVTCCRRNFP KQFLHYHRAG HGSVTSPQTQ
RGYTAFVHTK ISRVIGASGI HVGTMSFGKM EGDASDKNIA YMLQDDEADG PYYRQEWQGM
KETTPIISGG MNALRLPAFF ENLGHSNVIL TAGGGSFGHK DGPKIGAISC RQGEEAWKQW
KAGQFGNISL SDGVIEYAKT HEEIKGAFLT FQKDADQIYP GWKEKLGYTG ESSVQAASFD
WAKRASAAAF VGASVAPAKK ENVVARQALD QSSRYADLSL DEDTLIRNGK HVLVAYIMKP
KAGYDYLATA AHFAAESSTG TNVNVCTTDD FTKSVDALVY YIDPDNEEMK IAYPTLLFDR
NITDGRGMMC SFLTLAIGNN QGMGDVEYGK IYDFYLPPAF LRLYDGPSVN VEDMWRILGR
GTTNGGLVVG TIIKPKLGLQ PKPFGEACYS FWQGGDFIKN DEPQGNQVFC QMNECIPEVV
KAMRACVKET GSSKLFSANI TADDPEEMIA RGKYIMSQFG PLSENCAFLV DGYVAGGTAV
TCCRRNFPKQ FLHYHRAGHG SVTSPQTQRG YTAFVHTKIS RVIGASGIHV GTMSFGKMEG
DASDKNIAYM LQDDEADGPY YRQEWQGMKE TTPIISGGMN ALRLPAFFEN LGHSNVILTA
GGGSFGHKDG PKIGAISCRQ GEEAWKQWKA GQFGNISLSD GVIEYAKTHE EIKGAFLTFQ
KDADQIYPGW KEKLGYTGES SVQAASFDWA KRASAAAFVG ASVAPAKKEN VVARQALDQS
SRYADLSLDE DTLIRNGKHV LVAYIMKPKA GYDYLATAAH FAAESSTGTN VNVCTTDDFT
KSVDALVYYI DPDNEEMKIA YPTLLFDRNI TDGRGMMCSF LTLAIGNNQG MGDVEYGKIY
DFYLPPAFLR LYDGPSVNVE DMWRILGRGT TNGGLVVGTI IKPKLGLQPK PFGEACYSFW
QGGDFIKNDE PQGNQVFCQM NECIPEVVKA MRACVKETGS SKLFSANITA DDPEEMIARG
KYIMSQFGPL SENCAFLVDG YVAGGTAVTC CRRNFPKQFL HYHRAGHGSV TSPQTQRGYT
AFVHTKISRV IGASGIHVGT MSFGKMEGDA SDKNIAYMLQ DDEADGPYYR QEWQGMKETT
PIISGGMNAL RLPAFFENLG HSKVILTAGG GSFGHKDGPK IGAISCRQGE EAWKQWKAGQ
FGNISLSDGV IEYAKTHEEI KGAFLTFQKD ADQIYPGWKE KLGYTGESSV QAASFDWAKR
A
