ID E0WD02_9PHAE Unreviewed; 317 AA.
AC E0WD02;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:CAX11516.1};
OS Sphacelaria pulvinata.
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAX11516.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Sphacelariales; Sphacelariaceae; Sphacelaria.
OX NCBI_TaxID=588179 {ECO:0000313|EMBL:CAX11516.1};
RN [1] {ECO:0000313|EMBL:CAX11516.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1080/09670262.2010.490959;
RA Draisma S.G.A., Prud'homme van Reine W.F., Kawai H.;
RT "A revised classification of the Sphacelariales (Phaeophyceae) inferred
RT from a psbC and rbcL based phylogeny.";
RL Eur. J. Phycol. 45:308-326(2010).
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 -!- 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};
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DR EMBL; FM956114; CAX11516.1; -; Genomic_DNA.
DR AlphaFoldDB; E0WD02; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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 InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_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 SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 4: Predicted;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Chloroplast {ECO:0000313|EMBL:CAX11516.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:CAX11516.1}.
FT DOMAIN 1..294
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:CAX11516.1"
SQ SEQUENCE 317 AA; 34925 MW; 0251FFCC09CFCA6C CRC64;
PFLGATVKPK LGLSGKNYGR VVYEGLRGGL DFLKDDENIN SQPFMRWKER FLYCMEGVNR
AAAATGEVKG SYLNVTAATI EQMYERAEFA ESVGTVICMV DLVIGYTAIQ TMAIWARKAQ
MILHLHRAGN STYARQKNHG INFRVICKWM RMSGVDHIHA GTVVGKLEGD PLMVRGFYNT
LLLTELSVNL PEGLFFDMDW ASLRKCVPVA SGGIHCGQMH QLLYYLGDDV VLQFGGGTIG
HPDGIQSGAT ANRVALEAMV LARNEERDYV SQGPEILRVA AATCGPLKAA LDLWKDITFE
YTSTDTPDFV EVATESN
//
