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Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39)

 Q2PQH5_FUCVE            Unreviewed;       488 AA.
Q2PQH5;
24-JAN-2006, integrated into UniProtKB/TrEMBL.
24-JAN-2006, sequence version 1.
05-DEC-2018, entry version 80.
RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000313|EMBL:ABC25542.1};
ORFNames=FVCPDNA_045 {ECO:0000313|EMBL:CAX12442.1};
Fucus vesiculosus (Bladder wrack).
Plastid; Chloroplast {ECO:0000313|EMBL:ABC25542.1}.
Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Fucales; Fucaceae;
Fucus.
NCBI_TaxID=49266 {ECO:0000313|EMBL:ABC25542.1};
[1] {ECO:0000313|EMBL:ABC25542.1}
NUCLEOTIDE SEQUENCE.
Pearson G.A., Serrao E.A., Viegas C., Valente M.S.;
"The plastid genome sequence of the brown alga Fucus vesiculosus
(Phaeophyceae).";
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:CAX12442.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Vegetative tissue {ECO:0000313|EMBL:CAX12442.1};
PubMed=19835607; DOI=10.1186/1471-2148-9-253;
Le Corguille G., Pearson G., Valente M., Viegas C., Gschloessl B.,
Corre E., Bailly X., Peters A.F., Jubin C., Vacherie B., Cock J.M.,
Leblanc C.;
"Plastid genomes of two brown algae, Ectocarpus siliculosus and Fucus
vesiculosus: further insights on the evolution of red-algal derived
plastids.";
BMC Evol. Biol. 9:253-253(2009).
[3] {ECO:0000313|EMBL:CAX12442.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Vegetative tissue {ECO:0000313|EMBL:CAX12442.1};
Pearson G.A.;
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
ribulose 1,5-bisphosphate, the primary event in carbon dioxide
fixation, as well as the oxidative fragmentation of the pentose
substrate in the photorespiration process. Both reactions occur
simultaneously and in competition at the same active site.
{ECO:0000256|HAMAP-Rule:MF_01338}.
-!- CATALYTIC ACTIVITY:
Reaction=2 3-phospho-D-glycerate + 2 H(+) = CO2 + D-ribulose 1,5-
bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000256|HAMAP-
Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
-!- CATALYTIC ACTIVITY:
Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate +
3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
Evidence={ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
-!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
{ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
-!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
chain homodimer in a "head-to-tail" conformation. In form I
RuBisCO this homodimer is arranged in a barrel-like tetramer with
the small subunits forming a tetrameric "cap" on each end of the
"barrel". {ECO:0000256|HAMAP-Rule:MF_01338}.
-!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
subfamily. {ECO:0000256|HAMAP-Rule:MF_01338}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
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EMBL; DQ307680; ABC25542.1; -; Genomic_DNA.
EMBL; FM957154; CAX12442.1; -; Genomic_DNA.
RefSeq; YP_005090062.1; NC_016735.1.
ProteinModelPortal; Q2PQH5; -.
GeneID; 11542119; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
CDD; cd08212; RuBisCO_large_I; 1.
Gene3D; 3.20.20.110; -; 1.
Gene3D; 3.30.70.150; -; 1.
HAMAP; MF_01338; RuBisCO_L_type1; 1.
InterPro; IPR033966; RuBisCO.
InterPro; IPR020878; RuBisCo_large_chain_AS.
InterPro; IPR000685; RuBisCO_lsu_C.
InterPro; IPR036376; RuBisCO_lsu_C_sf.
InterPro; IPR017443; RuBisCO_lsu_fd_N.
InterPro; IPR036422; RuBisCO_lsu_N_sf.
InterPro; IPR020888; RuBisCO_lsuI.
PANTHER; PTHR42704; PTHR42704; 1.
Pfam; PF00016; RuBisCO_large; 1.
Pfam; PF02788; RuBisCO_large_N; 1.
SFLD; SFLDS00014; RuBisCO; 1.
SUPFAM; SSF51649; SSF51649; 1.
SUPFAM; SSF54966; SSF54966; 1.
PROSITE; PS00157; RUBISCO_LARGE; 1.
3: Inferred from homology;
Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Chloroplast {ECO:0000256|RuleBase:RU000302,
ECO:0000313|EMBL:ABC25542.1};
Lyase {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Plastid {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:ABC25542.1}.
DOMAIN 28 148 RuBisCO_large_N.
{ECO:0000259|Pfam:PF02788}.
DOMAIN 158 465 RuBisCO_large.
{ECO:0000259|Pfam:PF00016}.
ACT_SITE 179 179 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01338}.
ACT_SITE 297 297 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01338}.
METAL 205 205 Magnesium; via carbamate group.
{ECO:0000256|HAMAP-Rule:MF_01338}.
METAL 207 207 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01338}.
METAL 208 208 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 127 127 Substrate; in homodimeric partner.
{ECO:0000256|HAMAP-Rule:MF_01338}.
BINDING 177 177 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 181 181 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 298 298 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 330 330 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 382 382 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
SITE 337 337 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01338}.
MOD_RES 205 205 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_01338}.
SEQUENCE 488 AA; 53935 MW; C8D398894F319DF0 CRC64;
MPENVQERTR LKSERYESGV IPYAKMGYWD ADYNVKDTDI LALFRITPQP GVDPVEAAAA
VAGESSTATW TVVWTDLLTA CDIYRAKAYR VDPVPGTNDQ YFAYIAYECD LFEEGSLANL
TASIIGNVFG FKAVKALRLE DMRIPYAYLK TFQGPATGVI VERERLDKFG RPLLGATVKP
KLGLSGKNYG RVVYEGLTGG LDFLKDDENI NSQPFMRWKE RFLYCMEGVN RAAAATGEVK
GSYLNVTAAT MENMYERAEY SHAIGSVICM IDLVVGYTAI QSMAIWARKA EMILHLHRAG
NSTYARQKNH GINFRVICKW MRMCGVDHIH AGTVVGKLEG DPLMVKGFYN TLLLTELKIN
LAEGLFFDMD WASLRKCVPV ASGGIHCGQM HQLLYYLGDD VVLQFGGGTI GHPDGIQAGA
TANRVALEAM VLARNEGRDY VGEGPEILRT AASTCGPLKA ALDLWKDITF EYTSTDTPDF
TEVATESN


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