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Database: UniProt/SWISS-PROT
Entry: RBL_SOLLC
LinkDB: RBL_SOLLC
Original site: RBL_SOLLC 
ID   RBL_SOLLC               Reviewed;         477 AA.
AC   P27065; Q2A7G1; Q2MI92;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 4.
DT   31-JAN-2018, entry version 115.
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   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Solaneae; Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND93053816; DOI=10.2307/2399855;
RA   Olmstead R.G., Bremer B., Scott K.M., Palmer J.D.;
RT   "A parsimony analysis of the Asteridae sensu lato based on rbcL
RT   sequences.";
RL   Ann. Mo. Bot. Gard. 80:700-722(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. LA3023;
RX   PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA   Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T.,
RA   Guda C., Tomkins J., Jansen R.K.;
RT   "Complete chloroplast genome sequences of Solanum bulbocastanum,
RT   Solanum lycopersicum and comparative analyses with other Solanaceae
RT   genomes.";
RL   Theor. Appl. Genet. 112:1503-1518(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. IPA-6;
RX   PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA   Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT   "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT   solanaceous plastid genomes.";
RL   J. Mol. Evol. 63:194-207(2006).
RN   [4]
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: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2).
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; L14403; AAA19771.1; -; Unassigned_DNA.
DR   EMBL; DQ347959; ABC56308.1; -; Genomic_DNA.
DR   EMBL; AM087200; CAJ32401.1; -; Genomic_DNA.
DR   PIR; PQ0795; PQ0795.
DR   RefSeq; AP_004936.1; AC_000188.1.
DR   RefSeq; YP_008563096.1; NC_007898.3.
DR   ProteinModelPortal; P27065; -.
DR   SMR; P27065; -.
DR   STRING; 4081.Solyc01g007330.2.1; -.
DR   iPTMnet; P27065; -.
DR   PaxDb; P27065; -.
DR   PRIDE; P27065; -.
DR   EnsemblPlants; Solyc01g007330.2.1; Solyc01g007330.2.1; Solyc01g007330.2.
DR   GeneID; 3950460; -.
DR   Gramene; Solyc01g007330.2.1; Solyc01g007330.2.1; Solyc01g007330.2.
DR   KEGG; sly:3950460; -.
DR   eggNOG; ENOG410IIVP; Eukaryota.
DR   eggNOG; COG1850; LUCA.
DR   InParanoid; P27065; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; EOG093607MT; -.
DR   Proteomes; UP000004994; Chloroplast.
DR   ExpressionAtlas; P27065; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
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   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_0000031285.
FT   CHAIN         3    477       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031286.
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}.
SQ   SEQUENCE   477 AA;  52954 MW;  66CC07677A65C2B6 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PPAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQT ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFVEQDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVKA RNEGRDLARE GNEIIREACK WSPELAAACE VWKEIVFNFA AVDVLDK
//
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