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Database: UniProt/TrEMBL
Entry: C7B2G2_SELML
LinkDB: C7B2G2_SELML
Original site: C7B2G2_SELML 
ID   C7B2G2_SELML            Unreviewed;       475 AA.
AC   C7B2G2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   22-NOV-2017, entry version 36.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
DE            EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:ACT89000.1};
OS   Selaginella moellendorffii (Spikemoss).
OG   Plastid {ECO:0000313|EMBL:ACT89000.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19774466; DOI=10.1007/s11103-009-9545-3;
RA   Smith D.R.;
RT   "Unparalleled GC content in the plastid DNA of Selaginella.";
RL   Plant Mol. Biol. 71:627-639(2009).
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|RuleBase:RU000302}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2).
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU000302};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU000302};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU000302}.
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DR   EMBL; FJ755183; ACT89000.1; -; Genomic_DNA.
DR   RefSeq; YP_003097495.1; NC_013086.1.
DR   ProteinModelPortal; C7B2G2; -.
DR   STRING; 88036.ADH10411; -.
DR   PRIDE; C7B2G2; -.
DR   EnsemblPlants; ADH10411; ADH10411; ADH10411.
DR   GeneID; 8302288; -.
DR   Gramene; ADH10411; ADH10411; ADH10411.
DR   KEGG; smo:SemoP_p024; -.
DR   eggNOG; ENOG410IIVP; Eukaryota.
DR   eggNOG; COG1850; LUCA.
DR   InParanoid; C7B2G2; -.
DR   KO; K01601; -.
DR   Proteomes; UP000001514; Plastid.
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   Calvin cycle {ECO:0000256|RuleBase:RU000302};
KW   Carbon dioxide fixation {ECO:0000256|RuleBase:RU000302};
KW   Chloroplast {ECO:0000256|RuleBase:RU000302};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001514};
KW   Lyase {ECO:0000256|RuleBase:RU000302};
KW   Magnesium {ECO:0000256|RuleBase:RU000302};
KW   Metal-binding {ECO:0000256|RuleBase:RU000302};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000302};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000302};
KW   Photorespiration {ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000313|EMBL:ACT89000.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   DOMAIN       25    144       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      154    462       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ACT89000.1}.
SQ   SEQUENCE   475 AA;  51961 MW;  3CC536494E6846B1 CRC64;
     TSPQTETKAS VGSKAGVKDH RLTHYTPDYQ TKDTDIPAAS RMTPQPGVPA EEAGAAVAAE
     SSTGTWTTVW TDGLTNLDRY KGRCYDIEPV PGEKDQYIAY AAHPSDLSEE GSVTNMSTSI
     VGNVFGSKAL RAPRSEDLRI PPAYSKTSKG PPHGIQVERD KSNKYGRPSL GCTIKPKLGL
     SAKNYGRAVH ERLRGGLDFT KDDENVNPQP FMRWRDRFVF VAEALYKAQS ETGEIKGHHL
     NATAGTCEEM MKRAEFAREL GVPITMHDHS TGGFTANTSL AYYCRDNGLL PHIHRAMHAV
     IDRQKNHGIH FRVLAKASRM SGGDHIHGGT VVGKLEGERQ VTLGFVDLLR DDYIDKDRSR
     GIHPTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLAIE GNEVIREASK WSPELAAACE VWKEIKFEFE TIDTI
//
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