ID O78264_9FLOR Unreviewed; 427 AA.
AC O78264;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 22-FEB-2023, entry version 99.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
DE EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:AAC26599.1};
OS Torularia atra.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAC26599.1}.
OC Eukaryota; Rhodophyta; Florideophyceae; Nemaliophycidae; Batrachospermales;
OC Batrachospermaceae; Torularia.
OX NCBI_TaxID=2729737 {ECO:0000313|EMBL:AAC26599.1};
RN [1] {ECO:0000313|EMBL:AAC26599.1}
RP NUCLEOTIDE SEQUENCE.
RA Vis M.L., Saunders G.W., Sheath R.G., Dunse K., Entwisle T.J.;
RT "Phylogeny of the Batrachospermales (Rhodophyta) inferred from rbcL and 18S
RT ribosomal DNA gene sequences.";
RL J. Phycol. 34:341-350(1998).
RN [2] {ECO:0000313|EMBL:AAK01009.1}
RP NUCLEOTIDE SEQUENCE.
RA Vis M.L., Entwisle T.J.;
RT "Insights into the phylogeny of the Batrachospermales (Rhodophyta) from
RT rbcL sequence data of Australian taxa.";
RL J. Phycol. 36:1175-1182(2000).
RN [3] {ECO:0000313|EMBL:AIS76365.1}
RP NUCLEOTIDE SEQUENCE.
RA Abdelahad N., Bolpagni R., Jona Lasinio G., Vis M.L., Amadio C., Laini A.,
RA Keil E.J.;
RT "Distribution, morphology and ecological niche of Batrachospermum and
RT Sheathia species (Batrachospermales, Rhodophyta) in the fontanili of the Po
RT plain (northern Italy).";
RL Eur. J. Phycol. 50:318-329(2015).
RN [4] {ECO:0000313|EMBL:ANR02406.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27273531; DOI=10.1111/jpy.12401;
RA Entwisle T.J., Johnston E.T., Lam D.W., Stewart S.A., Vis M.L.;
RT "Nocturama gen. nov., Nothocladus s. lat. and other taxonomic novelties
RT resulting from the further resolution of paraphyly in Australasian members
RT of Batrachospermum (Batrachospermales, Rhodophyta).";
RL J. Phycol. 52:384-396(2016).
RN [5] {ECO:0000313|EMBL:QXU69866.1}
RP NUCLEOTIDE SEQUENCE.
RA Vis M.L., Entwisle T.J.;
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001067,
CC ECO:0000256|RuleBase:RU000302};
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:0000256|ARBA:ARBA00000537,
CC ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU000302}.
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; AF029139; AAC26599.1; -; Genomic_DNA.
DR EMBL; AF209979; AAK01009.1; -; Genomic_DNA.
DR EMBL; KM077029; AIS76365.1; -; Genomic_DNA.
DR EMBL; KT802842; ANR02406.1; -; Genomic_DNA.
DR EMBL; MW401957; QXU69866.1; -; Genomic_DNA.
DR AlphaFoldDB; O78264; -.
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 Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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 PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDG01052; RuBisCO; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567,
KW ECO:0000256|RuleBase:RU000302};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU000302};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:AAC26599.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000302};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000302};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000302};
KW Photorespiration {ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AAC26599.1}.
FT DOMAIN 2..94
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 107..411
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC26599.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:AAC26599.1"
SQ SEQUENCE 427 AA; 47218 MW; 23E850676B7ED6FC CRC64;
IEASAAIAGE SSTATWTVVW TDLLTACDLY RAKAYKVDAV PNTSDQYFAY IAYDIDLFEE
ASIANLTASI IGNVFGFKAV KALRLEDMRL PIAYLKTFQG PATGTIVERE RMDKFGRPFL
GATVKPKLGL SGKNYGRVVY EGLKGGLDFL KDDENINSQP FMRWRERFLF SIEGVNRAQA
AAGEIKGHYL NVTAATMEDM YERAEFAKEL GSIICMIDLV IGYTAIQSMA IWARKADMIL
HLHRAGNSTY SRQKIHGMNF RVICKWMRMA GVDHIHAGTV VGKLEGDPLM IKGFYDTLLL
SHLDINLPHG IFFEQNWASL RKVTPVASGG IHCGQMHQLL DYLGDDVVLQ FGGGTIGHPD
GIQAGATANR VALESMVMAR NEGRDYVNEG PQILRDAAKT CGPLQTALDL WKDISFNYTS
TDTADFV
//
