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

 A0A1C9CHR2_PLOCA        Unreviewed;       488 AA.
A0A1C9CHR2;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 1.
12-SEP-2018, entry version 12.
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:0000313|EMBL:AOM67899.1};
Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
ORFNames=Plocam_063 {ECO:0000313|EMBL:AOM67899.1};
Plocamium cartilagineum (Red comb weed) (Gelidium cartilagineum).
Plastid {ECO:0000313|EMBL:AOM67899.1}.
Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae;
Plocamiales; Plocamiaceae; Plocamium.
NCBI_TaxID=31452 {ECO:0000313|EMBL:AOM67899.1};
[1] {ECO:0000313|EMBL:AOM67899.1}
NUCLEOTIDE SEQUENCE.
PubMed=27589960; DOI=10.1186/s12915-016-0299-5;
Lee J., Cho C.H., Park S.I., Choi J.W., Song H.S., West J.A.,
Bhattacharya D., Yoon H.S.;
"Parallel evolution of highly conserved plastid genome architecture in
red seaweeds and seed plants.";
BMC Biol. 14:75-75(2016).
-!- 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. Both reactions occur simultaneously and in competition
at the same active site. {ECO:0000256|HAMAP-Rule:MF_01338}.
-!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP-
Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
-!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
D-ribulose 1,5-bisphosphate + O(2). {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}.
-!- 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}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
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EMBL; KX284727; AOM67899.1; -; Genomic_DNA.
RefSeq; YP_009297961.1; NC_031179.1.
GeneID; 29074356; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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};
Lyase {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01338,
ECO:0000256|RuleBase:RU000302}; Membrane {ECO:0000256|SAM:Phobius};
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|RuleBase:RU000302};
Photosynthesis {ECO:0000256|RuleBase:RU000302};
Plastid {ECO:0000256|RuleBase:RU000302};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 264 287 Helical. {ECO:0000256|SAM:Phobius}.
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; 54241 MW; 597A4AEB76AA78DB CRC64;
MSQSVEERTR IKNDRYESGV IPYAKMGYWD PDYTIKDTDI LAVFRVTPQP GVDPIEASAA
VAGESSTATW TVVWTDLLTA CDLYRAKAYK VDSVPNTSDQ YFAFIAYDID LFEEGSIANL
TASIIGNVFG FKAVKALRLE DMRIPVAYLK TFQGPATGII VERERMDKYG RPFLGATVKP
KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWKE RYLFSMEGVN RSIAAAGETK
GHYLNVTCAT IEEMYERAEF AKEIGSIIIM IDLVIGYTAI QTMAIWARKN DMILHLHRAG
NSTYSRQKIH GMNFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMIRGFYN TLLHTHLDIN
LPQGIFFEQD WASLRKVTPV ASGGIHCGQM HQLLDYLGDD VVLQFGGGTI GHPDGIQAGA
TANRVALESM VLARNEGRDY VNEGPQILQD AAKTCGPLQT ALDLWKDISF NYTSTDTADF
VETPTSST


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