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Database: UniProt/TrEMBL
Entry: D4PBB9_PHODC
LinkDB: D4PBB9_PHODC
Original site: D4PBB9_PHODC 
ID   D4PBB9_PHODC            Unreviewed;       484 AA.
AC   D4PBB9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   25-OCT-2017, entry version 53.
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:0000256|HAMAP-Rule:MF_01338,
GN   ECO:0000313|EMBL:ADD63179.1};
OS   Phoenix dactylifera (Date palm).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADD63179.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Arecaceae; Coryphoideae;
OC   Phoeniceae; Phoenix.
OX   NCBI_TaxID=42345 {ECO:0000313|EMBL:ADD63179.1};
RN   [1] {ECO:0000313|EMBL:ADD63179.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20856810; DOI=10.1371/journal.pone.0012762;
RA   Yang M., Zhang X., Liu G., Yin Y., Chen K., Yun Q., Zhao D.,
RA   Al-Mssallem I.S., Yu J.;
RT   "The complete chloroplast genome sequence of date palm (Phoenix
RT   dactylifera L.).";
RL   PLoS ONE 5:e12762-e12762(2010).
RN   [2] {ECO:0000313|EMBL:ADF28154.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DP00001 {ECO:0000313|EMBL:ADF28154.1};
RA   Khan A., Khan I.A., Heinze B., Azim M.K.;
RT   "The Chloroplast Genome Sequence of Date Palm (Phoenix dactylifera L.
RT   cv. Aseel).";
RL   Plant Mol. Biol. Rep. 30:666-678(2012).
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 in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site.
CC       {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 {ECO:0000256|HAMAP-
CC       Rule:MF_01338, 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; GU811709; ADD63179.1; -; Genomic_DNA.
DR   EMBL; FJ212316; ADF28154.1; -; Genomic_DNA.
DR   RefSeq; YP_003540939.1; NC_013991.2.
DR   GeneID; 8890518; -.
DR   KEGG; pda:8890518; -.
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:ADD63179.1};
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|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000313|EMBL:ADD63179.1}.
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;  53735 MW;  2E73F276493DA222 CRC64;
     MSCREGLMSP QTETKASVGF KAGVKDYKLT YYTPDYETKD TDILAAFRVT PQPGVPPEEA
     GAAVAAESST GTWTTVWTDG LTSLDRYKGR CYHIETVVGE ENQYIAYVAY PLDLFEEGSV
     TNMFTSIVGN VFGFKALRAL RLEDLRIPTS YSKTFQGPPH GIQVERDKLN KYGRPLLGCT
     IKPKLGLSAK NYGRAVYECL RGGLDFTKDD ENVNSQPFMR WRDRFVFCAE ALYKAQAETG
     EIKGHYLNAT AGTCEEMMKR AMCARELGVP IVMHDYLTGG FTANTSLAHY CRDNGLLLHI
     HRAMHAVIDR QKNHGMHFRV LAKALRMSGG DHIHAGTVVG KLEGEREMTL GFVDLLRDDF
     IEKDRSRGIF FTQDWVSMPG VLPVASGGIH VWHMPALTEI FGDDSVLQFG GGTLGHPWGN
     APGAVANRVA LEACVQARNE GRDLAREGNE IIREASKWSP ELAAACEVWK AIKFEFEPVD
     KLDK
//
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