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Database: UniProt/TrEMBL
Entry: E3VTZ5_THECC
LinkDB: E3VTZ5_THECC
Original site: E3VTZ5_THECC 
ID   E3VTZ5_THECC            Unreviewed;       484 AA.
AC   E3VTZ5; E3W0B6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 2.
DT   25-OCT-2017, entry version 48.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
DE            Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
GN   Name=rbcL {ECO:0000313|EMBL:ADO64817.2};
GN   Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
OS   Theobroma cacao (Cacao) (Cocoa).
OG   Plastid {ECO:0000313|EMBL:ADO64817.2}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae;
OC   Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:ADO64817.2};
RN   [1] {ECO:0000313|EMBL:ADO64817.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Sveinsson S., Kane N.C., Dempewolf H., Zhang D., Cronk Q.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEX57734.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kane N.C., Sveinsson S., Dempewolf H., Yang J.Y., Zhang D.,
RA   Engels J.M.M., Cronk Q.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AEX57734.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22301895; DOI=10.3732/ajb.1100570;
RA   Kane N., Sveinsson S., Dempewolf H., Yang J.Y., Zhang D., Engels J.M.,
RA   Cronk Q.;
RT   "Ultra-barcoding in cacao (Theobroma spp.; Malvaceae) using whole
RT   chloroplast genomes and nuclear ribosomal DNA.";
RL   Am. J. Bot. 99:320-329(2012).
RN   [4] {ECO:0000313|EMBL:ARJ62209.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang N., Handy S.M., Wen J.;
RT   "Plastid Genomes of Illicium.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition
CC       at the same active site. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with
CC       oxidative stress and protein turnover. {ECO:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In form I
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel". {ECO:0000256|HAMAP-Rule:MF_01338}.
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DR   EMBL; HQ244500; ADO64817.2; -; Genomic_DNA.
DR   EMBL; JQ228379; AEX57734.1; -; Genomic_DNA.
DR   EMBL; JQ228380; AEX57815.1; -; Genomic_DNA.
DR   EMBL; JQ228381; AEX57896.1; -; Genomic_DNA.
DR   EMBL; JQ228382; AEX57977.1; -; Genomic_DNA.
DR   EMBL; JQ228383; AEX58058.1; -; Genomic_DNA.
DR   EMBL; JQ228384; AEX58139.1; -; Genomic_DNA.
DR   EMBL; JQ228385; AEX58220.1; -; Genomic_DNA.
DR   EMBL; JQ228386; AEX58301.1; -; Genomic_DNA.
DR   EMBL; JQ228387; AEX58382.1; -; Genomic_DNA.
DR   EMBL; JQ228389; AEX58544.1; -; Genomic_DNA.
DR   EMBL; KY085907; ARJ62209.1; -; Genomic_DNA.
DR   RefSeq; YP_004021324.2; NC_014676.2.
DR   GeneID; 9978124; -.
DR   KEGG; tcc:9978124; -.
DR   KO; K01601; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 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   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020888; RuBisCO_lsuI.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Chloroplast {ECO:0000256|RuleBase:RU000302,
KW   ECO:0000313|EMBL:ADO64817.2};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Methylation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Photorespiration {ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000313|EMBL:ADO64817.2}.
FT   DOMAIN       31    151       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      161    469       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    182    182       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    301    301       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       208    208       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       210    210       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       211    211       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     130    130       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     184    184       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     302    302       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     334    334       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     386    386       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        341    341       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES      21     21       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     208    208       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    254    254       Interchain; in linked form.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
SQ   SEQUENCE   484 AA;  53752 MW;  DF5702C98C81897D CRC64;
     MSCREGLMSP QTETKASVGF KAGVKEYKLT YYTPEYEVKD TDILAAFRVT PQPGVPPEEA
     GAAVAAESST GTWTTVWTDG LTSLDRYKGR CYHIEPVAGE ENQYICYVAY PLDLFEEGSV
     TNMFTSIVGN VFGFKALRAL RLEDLRIPTA YIKTFQGPPH GIQVERDKLN KYGRPLLGCT
     IKPKLGLSAK NYGRAVYECL RGGLDFTKDD ENVNSQPFMR WRDRFLFCAE AIYKAQAETG
     EIKGHYLNAT AGTCEEMMKR AICARELGVP IVMHDYLTGG FTANTSLAHY CRDNGLLLHI
     HRAMHAVIDR QKNHGMHFRV LAKALRLSGG DHIHAGTVVG KLEGERDITL GFVDLLRDDF
     IEKDRSRGIY FTQDWVSIPG VLPVASGGIH VWHMPALTEI FGDDSVLQFG GGTLGHPWGN
     APGAVANRVA LEACVQARNE GRDLAREGNE IIREASKWSP ELAAACEVWK EIKFEFEAMD
     TLDK
//
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