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

 W6MDD6_ACEAT            Unreviewed;       485 AA.
W6MDD6;
16-APR-2014, integrated into UniProtKB/TrEMBL.
16-APR-2014, sequence version 1.
05-DEC-2018, entry version 27.
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:CDI27980.1};
Acetabularia acetabulum (Mermaid's wine glass) (Acetabularia
mediterranea).
Plastid; Chloroplast {ECO:0000313|EMBL:CDI27980.1}.
Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Dasycladales;
Polyphysaceae; Acetabularia.
NCBI_TaxID=35845 {ECO:0000313|EMBL:CDI27980.1};
[1] {ECO:0000313|EMBL:CDI27980.1}
NUCLEOTIDE SEQUENCE.
STRAIN=DI1 {ECO:0000313|EMBL:CDI27980.1};
Gould S.;
Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:CDI27980.1}
NUCLEOTIDE SEQUENCE.
STRAIN=DI1 {ECO:0000313|EMBL:CDI27980.1};
De Vries J., Habicht J., Woehle C., Changjie H., Christa G.,
Martin W.F., Gould S.B.;
"Is ftsH the key to plastid longevity in sacoglossan slugs?";
Submitted (FEB-2014) 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; HG518454; CDI27980.1; -; Genomic_DNA.
ProteinModelPortal; W6MDD6; -.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
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:CDI27980.1};
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};
Methylation {ECO:0000256|HAMAP-Rule:MF_01338};
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:CDI27980.1}.
DOMAIN 34 154 RuBisCO_large_N.
{ECO:0000259|Pfam:PF02788}.
DOMAIN 164 472 RuBisCO_large.
{ECO:0000259|Pfam:PF00016}.
ACT_SITE 185 185 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01338}.
ACT_SITE 304 304 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01338}.
METAL 211 211 Magnesium; via carbamate group.
{ECO:0000256|HAMAP-Rule:MF_01338}.
METAL 213 213 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01338}.
METAL 214 214 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 133 133 Substrate; in homodimeric partner.
{ECO:0000256|HAMAP-Rule:MF_01338}.
BINDING 183 183 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 187 187 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 305 305 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 337 337 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
BINDING 389 389 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01338}.
SITE 344 344 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01338}.
MOD_RES 24 24 N6,N6,N6-trimethyllysine.
{ECO:0000256|HAMAP-Rule:MF_01338}.
MOD_RES 211 211 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_01338}.
SEQUENCE 485 AA; 53878 MW; 331A491331D28769 CRC64;
MIEVFKNYYK NMGQTETKAG AGFKAGVKDY RLTYYTPDYQ VLDTDVLAAF RMTPQPGVPA
EECAAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDVEPV PGEENQYIAY VAYPLPLFEE
GSVTNLFTSI VGNVFGFKAL RALRLEDLRI PQSFVTTFLG PPHGIQVERD KLNKYGRSLL
GCTIKPKLGL SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKSQA
ETGEIKGHYL NATAPTSETM LQRAEVAKHL GVPIVMHDYL TAGFTANTSL ANYCRDHGLL
LHIHRAMHAV IDRQRNHGMH FRVLAKALRL SGGDHLHSGT VVGKLEGDRE VTMGFVDLMR
DDYIEKDRSR GIYFTQDWVG RGGVFPVASG GIHVWHMPAL VEIFGDDACL QFGGGTLGHP
WGNAPGAVAN RVALEACVQA RNEGRNLARE GGDIIRDAAK WSPELAAACE VWKEIKFEFD
IVDKL


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