RBL2_LINPO
ID RBL2_LINPO Reviewed; 547 AA.
AC Q42813; Q42814;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ribulose 1,5-bisphosphate carboxylase, chloroplastic;
DE EC=4.1.1.39;
DE Flags: Precursor; Fragment;
GN Name=rbcL;
OS Lingulodinium polyedra (Dinoflagellate) (Gonyaulax polyedra).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Gonyaulacales; Lingulodiniaceae;
OC Lingulodinium.
OX NCBI_TaxID=160621;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 144-153; 282-304;
RP 375-390 AND 437-461.
RC STRAIN=70;
RX PubMed=7777861; DOI=10.1126/science.7777861;
RA Morse D., Salois P., Markovic P., Hastings J.W.;
RT "A nuclear-encoded form II RuBisCO in dinoflagellates.";
RL Science 268:1622-1624(1995).
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. {ECO:0000250}.
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: It is not clear if this is the true start of the protein
CC or not; this is probably part of a polyprotein.
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; L41063; AAA98748.1; -; mRNA.
DR EMBL; L38610; AAC37234.1; -; mRNA.
DR AlphaFoldDB; Q42813; -.
DR SMR; Q42813; -.
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; 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 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; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..547
FT /note="Ribulose 1,5-bisphosphate carboxylase,
FT chloroplastic"
FT /id="PRO_0000042969"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 390
FT /note="Transition state stabilizer"
FT MOD_RES 252
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT CONFLICT 169..171
FT /note="SIG -> GTS (in Ref. 1; AAC37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="E -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="F -> L (in Ref. 1; AAC37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="V -> E (in Ref. 1; AAC37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="G -> D (in Ref. 1; AAC37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="K -> E (in Ref. 1; AAC37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="V -> I (in Ref. 1; AAC37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="N -> Y (in Ref. 1; AAA98748)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="T -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 547 AA; 59548 MW; F7AE4C6EAB921215 CRC64;
MGAFLTFQKD SDQIYPGWKE KLGYTGESSV QAASFDWQKK AAAAAFVGAQ ARTGRSTVVR
RALDQSSRYA DLSLTEEDLV KNGKHVLVAY IMNQGGYDYL ATAAHVAAES STGTNVNVCT
TDDFTKTVDA LVYYIDPENE EMKIAYPVPL FDRNITDGRA MMCSVLTLSI GNNQGMGDVE
YGKIYDIYFP PSYLRFFDGP ACSILDMWRI LGRDMTDGGL VVGTIIKPKL GLQPKPFGEA
CYAFGQGGDF IKNDEPQGNQ VFCQMNECIP EVVTAMKACI KETGSEKLFS ANITADDPAE
MIARGKYILG QFGPMAENCA FLVDGYVAGG TAVTVARRNF PKQFFHYHRA GHGAVTSPQT
QRGYTAFVHT KISRVIGASG IHVGTMSFGK MVGDASDKGI AYMLQQDAAG GPYYHQKWEG
VVQTTPIISG GMNALRLPAF FENLGHSNVI LTAGGGTFGH KDGPKQGATS CRQDEEAWKL
WKAGTYGDVS LSDGVIEYAK THEEIKGAFL TFQKDSDQIY PGWKEKLGYT GESSVQAASF
DWQKKAA
