ID G5EIB8_9PHAE Unreviewed; 438 AA.
AC G5EIB8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 22-FEB-2023, entry version 37.
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:BAL14476.1};
OS Padina maroensis.
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAL14476.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Dictyotales; Dictyotaceae; Padina.
OX NCBI_TaxID=659326 {ECO:0000313|EMBL:BAL14476.1};
RN [1] {ECO:0000313|EMBL:BAL14476.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HAW11 {ECO:0000313|EMBL:BAL14475.1}, HAW12
RC {ECO:0000313|EMBL:BAL14476.1}, and HAW13
RC {ECO:0000313|EMBL:BAL14477.1};
RA Ni-Ni-Win, Hanyuda T., Arai S., Uchimura M., Prathep A., Draisma S.G.,
RA Phang S.M., Abbott I.A., Millar A.J.K., Kawai H.;
RT "A taxonomic study of the genus Padina (Dictyotales, Phaeophyceae)
RT including the descriptions of four new species from Japan, Hawaii, and the
RT Andaman Sea.";
RL J. Phycol. 47:1193-1209(2011).
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}.
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DR EMBL; AB512541; BAL14475.1; -; Genomic_DNA.
DR EMBL; AB512542; BAL14476.1; -; Genomic_DNA.
DR EMBL; AB512543; BAL14477.1; -; Genomic_DNA.
DR AlphaFoldDB; G5EIB8; -.
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:BAL14476.1};
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:BAL14476.1}.
FT DOMAIN 1..98
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 108..415
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:BAL14476.1"
SQ SEQUENCE 438 AA; 48071 MW; C1734CE70DF056EE CRC64;
GVDPVEAAAA VAGESSTATW TVVWTDLLTA CDIYRAKAYR VDPVPGTNDQ FFAYIAYECD
LFEEGSLANL TASIIGNVFG FKAVKALRLE DMRIPYAYLK TFQGPATGVI VERERLDKFG
RPLLGATVKP KLGLSGKNYG RVVYEGLRGG LDFLKDDENI NSQPFMRWKE RFLYCMEGVN
RSAAATGEVK GSYLNVTAST IEQMYERAEY AEDIGTVIVM IDLVIGYTAI QTMAIWARKA
QMILHLHRAG NSTYARQKNH GINFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMVKGFYN
TLLLTELKVN LAEGLFFDMS WASLRKCVPV ASGGIHCGQM HQLLYYLGDD VVLQFGGGTI
GHPDGIQSGA TANRVALEAI VLARNEGRDY VAEGPELLRT AAATCAPLKT ALDLWKDITF
EYTSTDTPDF VEVPTGSP
//
