GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: RBL_VITVI C5MTM1_VITVI
LinkDB: RBL_VITVI C5MTM1_VITVI
Original site: RBL_VITVI C5MTM1_VITVI 
ID   RBL_VITVI               Reviewed;         475 AA.
AC   P56648; Q0ZJ12;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   22-NOV-2017, entry version 103.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE   Flags: Precursor;
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Vitis vinifera (Grape).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; Vitales; Vitaceae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Huang Y., Ma C., Li C.L., Wu N.H.;
RT   "Structure of the chloroplast rbcL gene from grape (Vitis vinifera).";
RL   Acta Bot. Sin. 36:444-451(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Maxxa;
RX   PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA   Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J.,
RA   Alverson A.J., Daniell H.;
RT   "Phylogenetic analyses of Vitis (Vitaceae) based on complete
RT   chloroplast genome sequences: effects of taxon sampling and
RT   phylogenetic methods on resolving relationships among rosids.";
RL   BMC Evol. Biol. 6:32-32(2006).
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:0000255|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:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01338};
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. {ECO:0000255|HAMAP-Rule:MF_01338}.
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:0000255|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:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
DR   EMBL; DQ424856; ABE47542.1; -; Genomic_DNA.
DR   PIR; A30610; A30610.
DR   RefSeq; YP_567084.1; NC_007957.1.
DR   ProteinModelPortal; P56648; -.
DR   SMR; P56648; -.
DR   STRING; 29760.VIT_07s0031g03000.t01; -.
DR   PRIDE; P56648; -.
DR   EnsemblPlants; VIT_07s0031g03000.t01; VIT_07s0031g03000.t01; VIT_07s0031g03000.
DR   GeneID; 4025045; -.
DR   Gramene; VIT_07s0031g03000.t01; VIT_07s0031g03000.t01; VIT_07s0031g03000.
DR   KEGG; vvi:4025045; -.
DR   InParanoid; P56648; -.
DR   KO; K01601; -.
DR   Proteomes; UP000009183; Chloroplast.
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   3: Inferred from homology;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Complete proteome; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW   Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome.
FT   PROPEP        1      2       {ECO:0000255|HAMAP-Rule:MF_01338}.
FT                                /FTId=PRO_0000031443.
FT   CHAIN         3    475       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031444.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       203    203       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     295    295       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     379    379       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES       3      3       N-acetylproline. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   MOD_RES      14     14       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   CONFLICT     32     32       K -> N (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    127    127       F -> V (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    154    155       GI -> RS (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    170    170       L -> I (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    226    226       F -> L (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    397    398       DS -> EF (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    412    414       GNA -> ETK (in Ref. 1). {ECO:0000305}.
SQ   SEQUENCE   475 AA;  52519 MW;  EF561118F2BE2B00 CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKPTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEESQFIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFVEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIRAASK WSPELAAACE VWKEIKFEFP AMDTL
//
  All links  
Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (23)   

Download RDF
ID   C5MTM1_VITVI            Unreviewed;       475 AA.
AC   C5MTM1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   22-NOV-2017, entry version 48.
DE   SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit {ECO:0000313|EMBL:ACS15220.1};
GN   Name=rbcL {ECO:0000313|EMBL:ACS15220.1};
OS   Vitis vinifera (Grape).
OG   Mitochondrion {ECO:0000313|EMBL:ACS15220.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; Vitales; Vitaceae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:ACS15220.1};
RN   [1] {ECO:0000313|EMBL:ACS15220.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PN40024 {ECO:0000313|EMBL:ACS15220.1};
RX   PubMed=20385587; DOI=10.1093/nar/gkq202;
RA   Picardi E., Horner D.S., Chiara M., Schiavon R., Valle G., Pesole G.;
RT   "Large-scale detection and analysis of RNA editing in grape mtDNA by
RT   RNA deep-sequencing.";
RL   Nucleic Acids Res. 38:4755-4767(2010).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; GQ220324; ACS15220.1; -; Genomic_DNA.
DR   RefSeq; YP_567084.1; NC_007957.1.
DR   ProteinModelPortal; C5MTM1; -.
DR   SMR; C5MTM1; -.
DR   PRIDE; C5MTM1; -.
DR   EnsemblPlants; VIT_07s0031g03000.t01; VIT_07s0031g03000.t01; VIT_07s0031g03000.
DR   GeneID; 4025045; -.
DR   Gramene; VIT_07s0031g03000.t01; VIT_07s0031g03000.t01; VIT_07s0031g03000.
DR   KEGG; vvi:4025045; -.
DR   KO; K01601; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
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   Mitochondrion {ECO:0000313|EMBL:ACS15220.1}.
FT   DOMAIN       24    144       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      154    462       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
SQ   SEQUENCE   475 AA;  52519 MW;  EF561118F2BE2B00 CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKPTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEESQFIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFVEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIRAASK WSPELAAACE VWKEIKFEFP AMDTL
//
  All links  
Ontology (4)   
   GO (4)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

Download RDF
DBGET integrated database retrieval system