RBL_PHYPA
ID RBL_PHYPA Reviewed; 475 AA.
AC P34915; Q95FY7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Flags: Precursor;
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kruse S., Martin W., Wehe M., Reski R.;
RT "An open reading frame (ycf11) is evolutionary conserved from Cyanobacteria
RT to the plastid DNAs of Archegoniates and Gymnosperms is modified in the
RT plastid DNAs of Dicots and is not plastome encoded in Monocots.";
RL J. Plant Physiol. 146:258-262(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Protonema;
RA Sugita M., Sugiura C.;
RT "Physcomitrella patens chloroplast genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=12954768; DOI=10.1093/nar/gkg726;
RA Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT evidence for the loss and relocation of rpoA from the chloroplast to the
RT nucleus.";
RL Nucleic Acids Res. 31:5324-5331(2003).
RN [4]
RP PROTEIN SEQUENCE OF 184-195.
RC TISSUE=Protonema;
RX PubMed=9129336; DOI=10.1007/s004250050065;
RA Kasten B., Buck F., Nuske J., Reski R.;
RT "Cytokinin affects nuclear- and plastome-encoded energy-converting plastid
RT enzymes.";
RL Planta 201:261-272(1997).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
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. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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:0000255|HAMAP-Rule:MF_01338}.
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'.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; X74156; CAA52269.1; -; Genomic_DNA.
DR EMBL; AB066207; BAB62086.1; -; Genomic_DNA.
DR EMBL; AP005672; BAC85044.1; -; Genomic_DNA.
DR PIR; S34663; S34663.
DR RefSeq; NP_904194.1; NC_005087.1.
DR AlphaFoldDB; P34915; -.
DR SMR; P34915; -.
DR PRIDE; P34915; -.
DR GeneID; 2546763; -.
DR KEGG; ppp:2546763; -.
DR InParanoid; P34915; -.
DR OrthoDB; 474428at2759; -.
DR Proteomes; UP000006727; Chloroplast.
DR GO; GO:0009507; C:chloroplast; 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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid; Reference proteome.
FT PROPEP 1..2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT /id="PRO_0000031347"
FT CHAIN 3..475
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031348"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 3
FT /note="N-acetylproline"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 14
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 9
FT /note="A -> T (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="Q -> H (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="A -> L (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="Y -> N (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="I -> L (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..256
FT /note="QF -> PC (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="L -> V (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="R -> L (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..374
FT /note="PGV -> QVF (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="W -> G (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> T (in Ref. 1; CAA52269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52705 MW; 30A91B8A714507AF CRC64;
MSPRPEIKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA EECGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYAIEPV AGEENQYIAY VAYPLDLFEE GSVTNLFTSI
VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQG ETGEIKGHYL
NATAGTCEEM IKRAQFAREL GMPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
LDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERQ VTLGFVDLLR DDYIEKDRSR
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFD TVDTL
