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

 RBL_MOROL               Reviewed;         466 AA.
P48708;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 83.
RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
Flags: Fragment;
Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
Moringa oleifera (Horseradish tree) (Moringa pterygosperma).
Plastid; Chloroplast.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Moringaceae; Moringa.
NCBI_TaxID=3735;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leaf;
AGRICOLA=IND93053815; DOI=10.2307/2399854;
Rodman J.E., Price R.A., Karol K.G., Conti E., Sytsma K., Palmer J.;
"Nucleotide sequences of the rbcL gene indicate monophyly of mustard
oil plants.";
Ann. Mo. Bot. Gard. 80:686-699(1993).
-!- 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:0000255|HAMAP-Rule:MF_01338}.
-!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
Rule:MF_01338}.
-!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
Rule:MF_01338}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_01338};
-!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
disulfide-linked. The disulfide link is formed within the large
subunit homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- PTM: The disulfide bond which can form in the large chain dimeric
partners within the hexadecamer appears to be associated with
oxidative stress and protein turnover. {ECO:0000255|HAMAP-
Rule:MF_01338}.
-!- 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:0000255|HAMAP-Rule:MF_01338}.
-!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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EMBL; L11359; AAA84457.2; -; Genomic_DNA.
ProteinModelPortal; P48708; -.
SMR; P48708; -.
PRIDE; P48708; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
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.
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; Carbon dioxide fixation; Chloroplast; Disulfide bond;
Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase;
Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
CHAIN <1 466 Ribulose bisphosphate carboxylase large
chain.
/FTId=PRO_0000062533.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01338}.
ACT_SITE 285 285 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01338}.
METAL 192 192 Magnesium; via carbamate group.
{ECO:0000255|HAMAP-Rule:MF_01338}.
METAL 194 194 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01338}.
METAL 195 195 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01338}.
BINDING 114 114 Substrate; in homodimeric partner.
{ECO:0000255|HAMAP-Rule:MF_01338}.
BINDING 164 164 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01338}.
BINDING 168 168 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01338}.
BINDING 286 286 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01338}.
BINDING 318 318 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01338}.
BINDING 370 370 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01338}.
SITE 325 325 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01338}.
MOD_RES 5 5 N6,N6,N6-trimethyllysine.
{ECO:0000255|HAMAP-Rule:MF_01338}.
MOD_RES 192 192 N6-carboxylysine. {ECO:0000255|HAMAP-
Rule:MF_01338}.
DISULFID 238 238 Interchain; in linked form.
{ECO:0000255|HAMAP-Rule:MF_01338}.
NON_TER 1 1
SEQUENCE 466 AA; 51585 MW; 4763F9F6CC90E776 CRC64;
SVGFKAGVKD YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV
WTDGLTSLDR YKGRCYHIEP IAGEENQFIA YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA
LRALRLEDLR IPPAYSKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEAIYKAQ AETGEIKGHY LNATAGTCEE
MIKRAVFARE LGAPIIMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM
HFRVLAKALR LSGGDHIHAG TVVGKLEGER EITLGFVDLL RDDFVEKDRS RGIFFTQDWV
SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ
ARNEGRDLAR EGNEIIRKAS KWSPELAAAC EVWKEIKFEF PAVDTL


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