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Database: UniProt/SWISS-PROT
Entry: RBL_SOYBN
LinkDB: RBL_SOYBN
Original site: RBL_SOYBN 
ID   RBL_SOYBN               Reviewed;         475 AA.
AC   P27066; Q2PMV1;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 3.
DT   05-DEC-2018, entry version 110.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=rbcL;
OS   Glycine max (Soybean) (Glycine hispida).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
OC   Phaseoleae; Glycine; Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   PubMed=9242596; DOI=10.1006/mpev.1997.0410;
RA   Kaess E., Wink M.;
RT   "Phylogenetic relationships in the Papilionoideae (family Leguminosae)
RT   based on nucleotide sequences of cpDNA (rbcL) and ncDNA (ITS 1 and
RT   2).";
RL   Mol. Phylogenet. Evol. 8:65-88(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PI 437654;
RX   PubMed=16247559; DOI=10.1007/s11103-005-8882-0;
RA   Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G.,
RA   Jansen R.K.;
RT   "Complete chloroplast genome sequence of Glycine max and comparative
RT   analyses with other legume genomes.";
RL   Plant Mol. Biol. 59:309-322(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, AND ACETYLATION AT
RP   PRO-3.
RX   PubMed=16668742; DOI=10.1104/pp.98.3.1170;
RA   Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.;
RT   "Posttranslational modifications in the amino-terminal region of the
RT   large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from
RT   several plant species.";
RL   Plant Physiol. 98:1170-1174(1992).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 3-phospho-D-glycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC       disulfide-linked. The disulfide link is formed within the large
CC       subunit homodimers (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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:0000250}.
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" (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
DR   EMBL; Z95552; CAB08877.1; -; Genomic_DNA.
DR   EMBL; DQ317523; ABC25107.1; -; Genomic_DNA.
DR   RefSeq; YP_538747.1; NC_007942.1.
DR   ProteinModelPortal; P27066; -.
DR   SMR; P27066; -.
DR   iPTMnet; P27066; -.
DR   PRIDE; P27066; -.
DR   GeneID; 3989271; -.
DR   KEGG; gmx:3989271; -.
DR   InParanoid; P27066; -.
DR   KO; K01601; -.
DR   Proteomes; UP000008827; Chloroplast.
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   PANTHER; PTHR42704; PTHR42704; 1.
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   1: Evidence at protein level;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Complete proteome; Direct protein sequencing; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase;
KW   Photorespiration; Photosynthesis; Plastid; Reference proteome.
FT   PROPEP        1      2       {ECO:0000269|PubMed:16668742}.
FT                                /FTId=PRO_0000031411.
FT   CHAIN         3    475       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031412.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000250}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       203    203       Magnesium. {ECO:0000250}.
FT   METAL       204    204       Magnesium. {ECO:0000250}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000250}.
FT   BINDING     173    173       Substrate. {ECO:0000250}.
FT   BINDING     177    177       Substrate. {ECO:0000250}.
FT   BINDING     295    295       Substrate. {ECO:0000250}.
FT   BINDING     327    327       Substrate. {ECO:0000250}.
FT   BINDING     379    379       Substrate. {ECO:0000250}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   MOD_RES       3      3       N-acetylproline.
FT                                {ECO:0000269|PubMed:16668742}.
FT   MOD_RES      14     14       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000269|PubMed:16668742}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000250}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000250}.
FT   CONFLICT    143    143       A -> S (in Ref. 1; CAB08877).
FT                                {ECO:0000305}.
FT   CONFLICT    470    470       E -> P (in Ref. 1; CAB08877).
FT                                {ECO:0000305}.
FT   CONFLICT    474    475       Missing (in Ref. 1; CAB08877).
FT                                {ECO:0000305}.
SQ   SEQUENCE   475 AA;  52610 MW;  481460745D587783 CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYGLEPV AGEENQYIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PTAYIKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL
     NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRL SGGDHVHAGT VVGKLEGERE ITLGFVDLLR DDFVEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE VWKEIKFEFE AMDTL
//
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