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Entry: RBL_SOLTU A0A0N7CI26_SOLTU
LinkDB: RBL_SOLTU A0A0N7CI26_SOLTU
Original site: RBL_SOLTU A0A0N7CI26_SOLTU 
ID   RBL_SOLTU               Reviewed;         477 AA.
AC   P25079; Q27S42; Q2VEG9;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   20-DEC-2017, 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   Solanum tuberosum (Potato).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16668878; DOI=10.1104/pp.99.1.356;
RA   Enyedi A.J., Pell E.J.;
RT   "Comparison of the rbcL gene sequence of two potato cultivars with
RT   differential sensitivity to ozone.";
RL   Plant Physiol. 99:356-358(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Desiree;
RX   PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA   Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA   Jeong W.-J., Liu J.R.;
RT   "The complete chloroplast genome sequences of Solanum tuberosum and
RT   comparative analysis with Solanaceae species identified the presence
RT   of a 241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL   Plant Cell Rep. 25:1369-1379(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Desiree;
RA   Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S.,
RA   Cardi T.;
RT   "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT   Desiree and comparative analyses with other Solanaceae genomes.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; M76402; AAB01597.1; -; Genomic_DNA.
DR   EMBL; DQ231562; ABB90049.1; -; Genomic_DNA.
DR   EMBL; DQ386163; ABD47065.1; -; Genomic_DNA.
DR   PIR; PQ0797; PQ0797.
DR   RefSeq; YP_635647.1; NC_008096.2.
DR   ProteinModelPortal; P25079; -.
DR   SMR; P25079; -.
DR   STRING; 4113.PGSC0003DMT400083063; -.
DR   iPTMnet; P25079; -.
DR   PRIDE; P25079; -.
DR   GeneID; 4099985; -.
DR   KEGG; sot:4099985; -.
DR   eggNOG; ENOG410IIVP; Eukaryota.
DR   eggNOG; COG1850; LUCA.
DR   InParanoid; P25079; -.
DR   KO; K01601; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P25079; baseline.
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_0000031409.
FT   CHAIN         3    477       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031410.
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     26     26       T -> P (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT     83     83       R -> S (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    217    217       R -> L (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    226    226       F -> Y (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    262    262       T -> V (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    273    273       G -> A (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    306    306       N -> S (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    377    377       V -> E (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
FT   CONFLICT    449    449       A -> C (in Ref. 1; AAB01597).
FT                                {ECO:0000305}.
SQ   SEQUENCE   477 AA;  52944 MW;  46E2EC09C2619F72 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMLTSI
     VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQA ETGEIKGHYL
     NATAGTCEEM MKRAVFAREL GTPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFIEQDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVKA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIVFNFA AMDVLDK
//
ID   A0A0N7CI26_SOLTU        Unreviewed;       477 AA.
AC   A0A0N7CI26;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-MAR-2018, entry version 21.
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:AKM22039.1};
OS   Solanum tuberosum (Potato).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AKM22039.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EMBL:AKM22039.1};
RN   [1] {ECO:0000313|EMBL:AKM22039.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cho K.-S., Kim K.-H., Yang T.-J.;
RT   "To survey the complete chloroplast genome of Solanum tuberosum.";
RL   Submitted (JAN-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 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   -!- 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; KM489056; AKM22039.1; -; Genomic_DNA.
DR   RefSeq; YP_635647.1; NC_008096.2.
DR   ProteinModelPortal; A0A0N7CI26; -.
DR   SMR; A0A0N7CI26; -.
DR   GeneID; 4099985; -.
DR   KEGG; sot:4099985; -.
DR   KO; K01601; -.
DR   ExpressionAtlas; A0A0N7CI26; baseline.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-UniRule.
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:AKM22039.1};
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:AKM22039.1}.
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   477 AA;  52944 MW;  46E2EC09C2619F72 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMLTSI
     VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQA ETGEIKGHYL
     NATAGTCEEM MKRAVFAREL GTPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFIEQDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVKA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIVFNFA AMDVLDK
//
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