RBL2_PROMN
ID RBL2_PROMN Reviewed; 1563 AA.
AC Q6Y9H0; Q6Y9I0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase 4;
DE Flags: Precursor; Fragment;
GN Name=rbcL;
OS Prorocentrum minimum (Dinoflagellate) (Exuviaella minima).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Prorocentrales; Prorocentraceae;
OC Prorocentrum.
OX NCBI_TaxID=39449;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE COPY, AND DETECTION OF PROTEIN.
RC STRAIN=CCMP696 / 1PM;
RA Zhang H., Lin S.;
RT "Complex gene structure of the form II Rubisco in the dinoflagellate
RT Prorocentrum minimum (Dinophyceae).";
RL J. Phycol. 39:1160-1171(2003).
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 -!- PTM: In Western blots an approximately 220 kDa polyprotein and 2
CC smaller proteins of about 55 and 52 kDa are detected, suggesting the
CC polyprotein may be cleaved at one end of the linker and then at the
CC other end to give mature RuBisCO.
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 220 kDa polyprotein,
CC imported into chloroplasts and subsequently cleaved into 4 mature
CC RuBisCO proteins. Only the 2 middle RuBisCO copies are complete in this
CC entry. There are estimated to be at least 10 copies of this polyprotein
CC gene.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY169179; AAO13036.1; -; mRNA.
DR EMBL; AY169169; AAO13026.1; -; mRNA.
DR AlphaFoldDB; Q6Y9H0; -.
DR SMR; Q6Y9H0; -.
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; 2.
DR Gene3D; 3.20.20.110; -; 4.
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; 4.
DR Pfam; PF00016; RuBisCO_large; 4.
DR Pfam; PF02788; RuBisCO_large_N; 3.
DR SUPFAM; SSF51649; SSF51649; 4.
DR SUPFAM; SSF54966; SSF54966; 3.
DR PROSITE; PS00157; RUBISCO_LARGE; 3.
PE 2: Evidence at transcript level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid; Repeat.
FT CHAIN <1..196
FT /note="Ribulose bisphosphate carboxylase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042971"
FT PROPEP 197..217
FT /note="Linker"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042972"
FT CHAIN 218..702
FT /note="Ribulose bisphosphate carboxylase 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042973"
FT PROPEP 703..723
FT /note="Linker"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042974"
FT CHAIN 724..1208
FT /note="Ribulose bisphosphate carboxylase 3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042975"
FT PROPEP 1209..1229
FT /note="Linker"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042976"
FT CHAIN 1230..>1563
FT /note="Ribulose bisphosphate carboxylase 4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042977"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 504
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 889
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1010
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1395
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1516
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 410
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 891
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 914
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 916
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 917
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1011
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1044
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1091
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1340
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 1397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 1517
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1550
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 40
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 546
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 1052
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 1558
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 408
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT MOD_RES 914
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT MOD_RES 1420
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT CONFLICT 702
FT /note="D -> E (in Ref. 1; AAO13026)"
FT /evidence="ECO:0000305"
FT CONFLICT 712..713
FT /note="TT -> KA (in Ref. 1; AAO13026)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="A -> T (in Ref. 1; AAO13026)"
FT /evidence="ECO:0000305"
FT CONFLICT 1208
FT /note="D -> E (in Ref. 1; AAO13026)"
FT /evidence="ECO:0000305"
FT CONFLICT 1218..1221
FT /note="TTRK -> KART (in Ref. 1; AAO13026)"
FT /evidence="ECO:0000305"
FT CONFLICT 1226
FT /note="A -> T (in Ref. 1; AAO13026)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 1563
SQ SEQUENCE 1563 AA; 169955 MW; 071A3E54EF7D81AF CRC64;
GHGAVTSPQT QRGYTAFVHT KLSRVIGASG IHTGTMSFGK MEGDASDKNI GFMLQDDVAD
GPYYRQEWEG MKQTTPIISG GMNALRLPAF FENLGHSNVI LTAGGGAFGH KDGPKQGAIS
CAQGEESWKL WKAGTYGDVS LSDGVVEYAK THEELKGAFL TFQKDADQIY PGWKEKLGYT
GESSVQAASF NWQKKDLAAA FVGASTTRKA SSVARRALDQ SSRYADLSLT EEDLIKNGQH
VLVAYIMKPK AGYDYLATAA HFAAESSTGT NVNVCTTDDF TKTVDALVYY IDPENEEMKI
AYPTALFDRN ITDGRAMMCS VLTLSIGNNQ GMGDVDYGKI YDIYFPPQYL RLFDGPSCCV
IDMWRILGRG TVGGGLVVGT IIKPKLGLQP KPFGQACYGF WQGGDFIKND EPQGNQTFCQ
MNECIPEVVK AMRAAQEETG QGKLFSANIT ADDPNEMIAR AKYILNQMGP MAENCAFLVD
GYVAGGTAVT VARRNFPKQF LHYHRAGHGA VTSPQTQRGY TAFVHTKLSR VIGASGIHTG
TMSFGKMEGD ASDKNIGFML QDDVADGPYY RQEWEGMKQT TPIISGGMNA LRLPAFFENL
GHSNVILTAG GGAFGHKDGP KQGAISCAQG EESWKLWKAG TYGDVSLSDG VVEYAKTHEE
LKGAFLTFQK DADQIYPGWK EKLGYTGESS VQAASFNWQK KDLAAAFVGA STTRKASSVA
RRALDQSSRY ADLSLTEEDL IKNGQHVLVA YIMKPKAGYD YLATAAHFAA ESSTGTNVNV
CTTDDFTKTV DALVYYIDPE NEEMKIAYPT ALFDRNITDG RAMMCSVLTL SIGNNQGMGD
VDYGKIYDIY FPPQYLRLFD GPSCCVIDMW RILGRGTVGG GLVVGTIIKP KLGLQPKPFG
QACYGFWQGG DFIKNDEPQG NQTFCQMNEC IPEVVKAMRA AQEETGQGKL FSANITADDP
NEMIARAKYI LNQMGPMAEN CAFLVDGYVA GGTAVTVARR NFPKQFLHYH RAGHGAVTSP
QTQRGYTAFV HTKLSRVIGA SGIHTGTMSF GKMEGDASDK NIGFMLQDDV ADGPYYRQEW
EGMKQTTPII SGGMNALRLP AFFENLGHSN VILTAGGGAF GHKDGPKQGA ISCAQGEESW
KLWKAGTYGD VSLSDGVVEY AKTHEELKGA FLTFQKDADQ IYPGWKEKLG YTGESSVQAA
SFNWQKKDLA AAFVGASTTR KASSVARRAL DQSSRYADLS LTEEDLIKNG QHVLVAYIMK
PKAGYDYLAT AAHFAAESST GTNVNVCTTD DFTKTVDALV YYIDPENEEM KIAYPTALFD
RNITDGRAMM CSVLTLSIGN NQGMGDVDYG KIYDIYFPPQ YLRLFDGPSC CVIDMWRILG
RGTVGGGLVV GTIIKPKLGL QPKPFGQACY GFWQGGDFIK NDEPQGNQTF CQMNECIPEV
VKAMRAAQEE TGQGKLFSAN ITADDPNEMI ARAKYILNQM GPMAENCAFL VDGYVAGGTA
VTVARRNFPK QFLHYHRAGH GAVTSPQTQR GYTAFVHTKL SRVIGASGIH TGTMSFGKME
GDA
