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Database: UniProt/TrEMBL
Entry: D3WC82_NELNU
LinkDB: D3WC82_NELNU
Original site: D3WC82_NELNU 
ID   D3WC82_NELNU            Unreviewed;       475 AA.
AC   D3WC82;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   25-OCT-2017, entry version 59.
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:ADD29858.1, ECO:0000313|RefSeq:YP_009093958.1};
GN   ORFNames=N623_p057 {ECO:0000313|RefSeq:YP_009093958.1}, NenuCp029
GN   {ECO:0000313|EMBL:ACN49416.1};
OS   Nelumbo nucifera (Sacred lotus).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADD29858.1,
OG   ECO:0000313|RefSeq:YP_009093958.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Proteales;
OC   Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|EMBL:ADD29858.1};
RN   [1] {ECO:0000313|EMBL:ACN49416.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Quan Z., Ding Y.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADD29858.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20176954; DOI=10.1073/pnas.0907801107;
RA   Moore M.J., Soltis P.S., Bell C.D., Burleigh J.G., Soltis D.E.;
RT   "Phylogenetic analysis of 83 plastid genes further resolves the early
RT   diversification of eudicots.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:4623-4628(2010).
RN   [3] {ECO:0000313|EMBL:AFH01455.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xue J., Wang S., Zhou S.-L.;
RT   "Polymorphic Chloroplast Microsatellite loci in Nelumbo
RT   (Nalumbonaceae).";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000189703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. China Antique {ECO:0000313|Proteomes:UP000189703};
RX   PubMed=23663246; DOI=10.1186/gb-2013-14-5-r41;
RA   Ming R., VanBuren R., Liu Y., Yang M., Han Y., Li L.T., Zhang Q.,
RA   Kim M.J., Schatz M.C., Campbell M., Li J., Bowers J.E., Tang H.,
RA   Lyons E., Ferguson A.A., Narzisi G., Nelson D.R., Blaby-Haas C.E.,
RA   Gschwend A.R., Jiao Y., Der J.P., Zeng F., Han J., Min X.J.,
RA   Hudson K.A., Singh R., Grennan A.K., Karpowicz S.J., Watling J.R.,
RA   Ito K., Robinson S.A., Hudson M.E., Yu Q., Mockler T.C., Carroll A.,
RA   Zheng Y., Sunkar R., Jia R., Chen N., Arro J., Wai C.M., Wafula E.,
RA   Spence A., Han Y., Xu L., Zhang J., Peery R., Haus M.J., Xiong W.,
RA   Walsh J.A., Wu J., Wang M.L., Zhu Y.J., Paull R.E., Britt A.B., Du C.,
RA   Downie S.R., Schuler M.A., Michael T.P., Long S.P., Ort D.R.,
RA   Schopf J.W., Gang D.R., Jiang N., Yandell M., dePamphilis C.W.,
RA   Merchant S.S., Paterson A.H., Buchanan B.B., Li S., Shen-Miller J.;
RT   "Genome of the long-living sacred lotus (Nelumbo nucifera Gaertn.).";
RL   Genome Biol. 14:R41-R41(2013).
RN   [5] {ECO:0000313|EMBL:AGO98532.1, ECO:0000313|RefSeq:YP_009093958.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Peery R.M., VanBuren R., Han J.O., Downie S.R., Ming R.;
RT   "The organelle genomes of Nelumbo nucifera.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|RefSeq:YP_009093958.1}
RP   NUCLEOTIDE SEQUENCE.
RG   NCBI Genome Project;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:ALO23541.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|RefSeq:YP_009093958.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAY-2017) to UniProtKB.
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; FJ754270; ACN49416.1; -; Genomic_DNA.
DR   EMBL; GQ997596; ADD29858.1; -; Genomic_DNA.
DR   EMBL; JQ336993; AFH01455.1; -; Genomic_DNA.
DR   EMBL; KF009944; AGO98532.1; -; Genomic_DNA.
DR   EMBL; KT119345; ALO23541.1; -; Genomic_DNA.
DR   EMBL; KT119346; ALO23542.1; -; Genomic_DNA.
DR   RefSeq; YP_009093958.1; NC_025339.1.
DR   GeneID; 10743890; -.
DR   KEGG; nnu:10743890; -.
DR   KO; K01601; -.
DR   Proteomes; UP000189703; Genome assembly.
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:ADD29858.1, ECO:0000313|RefSeq:YP_009093958.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000189703};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302,
KW   ECO:0000313|EMBL:ALO23541.1};
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:ADD29858.1,
KW   ECO:0000313|RefSeq:YP_009093958.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT   DOMAIN       24    144       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      154    462       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       203    203       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     295    295       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     327    327       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     379    379       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES      14     14       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
SQ   SEQUENCE   475 AA;  52685 MW;  949FF713FFD166FD CRC64;
     MSPQTETKAS VGFKAGVKDY RLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEESQFIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE VWKEIKFEFE AMDTL
//
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