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Database: UniProt/SWISS-PROT
Entry: RBL_PARDP
LinkDB: RBL_PARDP
Original site: RBL_PARDP 
ID   RBL_PARDP               Reviewed;         487 AA.
AC   A1B2Q2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   10-OCT-2018, entry version 74.
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};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=Pden_1699;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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. Both reactions occur simultaneously and in competition
CC       at the same active site. {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       {ECO:0000255|HAMAP-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; CP000489; ABL69796.1; -; Genomic_DNA.
DR   RefSeq; WP_011747994.1; NC_008686.1.
DR   ProteinModelPortal; A1B2Q2; -.
DR   SMR; A1B2Q2; -.
DR   STRING; 318586.Pden_1699; -.
DR   PRIDE; A1B2Q2; -.
DR   EnsemblBacteria; ABL69796; ABL69796; Pden_1699.
DR   KEGG; pde:Pden_1699; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; PDEN318586:G1GW1-1700-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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: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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    487       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000299967.
FT   ACT_SITE    179    179       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    297    297       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       205    205       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       207    207       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       208    208       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     127    127       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     181    181       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     298    298       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     330    330       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     382    382       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        337    337       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     205    205       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   487 AA;  53971 MW;  07BD6810EEA63615 CRC64;
     MNEMSKSEIT DKKKRYAAGV LKYAQMGYWD GDYQPKDTDI LALFRITPQD GVDPIEAAAA
     VAGESSTATW TVVWTDRLTA CDQYRAKAYK VEPVPGQEGQ YFCYVAYDLI LFEEGSIANV
     TASIIGNVFS FKPLLAARLE DMRFPVAYMK TFAGPPTGIV VERERLDKFG RPLLGATTKP
     KLGLSGKNYG RVVYEGLKGG LDFMKDDENI NSQPFMHWRD RFLYCMEAVN KATAVTGEVK
     GHYLNITAGT MEEMYRRAEL AKELGSVIVM VDLIVGWTAI QSISNWCRQN DMILHMHRAG
     HGTYTRQKNH GISFRVIAKW LRMAGVDHLH CGTAVGKLEG DPLTVQGYYN TCREMVNEVD
     LPRGIFFEQD WGNLKKVMPV ASGGIHAGQM HQLLDLFGDD VVLQFGGGTI GHPMGIQAGA
     TANRVALEAM VLARNEGVDL KTEGPEVLRR AAKWCKPLEA ALDVWGNITF NYTSTDTSDF
     VPTASVS
//
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