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Database: UniProt/SWISS-PROT
Entry: RBL_BRADU
LinkDB: RBL_BRADU
Original site: RBL_BRADU 
ID   RBL_BRADU               Reviewed;         486 AA.
AC   Q9ZI34; Q79UA8; Q8GKR7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   05-DEC-2018, entry version 104.
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, ECO:0000269|PubMed:9882445};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=blr2585;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC
OS   14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=BJ110;
RX   PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA   Horken K.M., Tabita F.R.;
RT   "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT   molecules that possess different CO2/O2 substrate specificities.";
RL   Arch. Biochem. Biophys. 361:183-194(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fischer H.-M., Bauer E., Hennecke H.;
RT   "The Bradyrhizobium japonicum cbb locus.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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:0000269|PubMed:9882445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 3-phospho-D-glycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338, ECO:0000269|PubMed:9882445};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338,
CC         ECO:0000269|PubMed:9882445};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=55 uM for ribulose 1,5-bisphosphate
CC         {ECO:0000269|PubMed:9882445};
CC         KM=66 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC         Vmax=2.8 umol/min/mg enzyme with CO(2) as substrate
CC         {ECO:0000269|PubMed:9882445};
CC         Note=The CO(2)/O(2) specificity factor (tau) is 75.;
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:9882445}.
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; AF041820; AAD05386.1; -; Genomic_DNA.
DR   EMBL; AY150332; AAN61148.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC47850.1; -; Genomic_DNA.
DR   RefSeq; NP_769225.1; NC_004463.1.
DR   ProteinModelPortal; Q9ZI34; -.
DR   SMR; Q9ZI34; -.
DR   STRING; 224911.blr2585; -.
DR   PRIDE; Q9ZI34; -.
DR   EnsemblBacteria; BAC47850; BAC47850; BAC47850.
DR   GeneID; 1049510; -.
DR   KEGG; bja:blr2585; -.
DR   PATRIC; fig|224911.5.peg.2551; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   InParanoid; Q9ZI34; -.
DR   KO; K01601; -.
DR   OMA; FTQDWAS; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; BDIA224911:G1G3J-2608-MONOMER; -.
DR   SABIO-RK; Q9ZI34; -.
DR   Proteomes; UP000002526; Chromosome.
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   1: Evidence at protein level;
KW   Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    486       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062620.
FT   ACT_SITE    177    177       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    295    295       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       203    203       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       205    205       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       206    206       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     125    125       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     175    175       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     179    179       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     296    296       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     328    328       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     380    380       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        335    335       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     203    203       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   CONFLICT     87     87       H -> Y (in Ref. 1; AAN61148/BAC47850).
FT                                {ECO:0000305}.
SQ   SEQUENCE   486 AA;  53818 MW;  4E949E13F57FDCE7 CRC64;
     MNAHTGTVRG KERYRSGVME YKRMGYWEPD YTPKDTDVIA LFRVTPQEGV DPIEASAAVA
     GESSTATWTV VWTDRLTAAE KYRAKCHRVD PVPGTPGSYF AYIAYDLDLF EPGSIANLSA
     SIIGNVFGFK PLKALRLEDM RFPVAYVKTF QGPATGIVVE RERLDKFGRP LLGATVKPKL
     GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRDRF LYCIEAVNRA QAASGEVKGT
     YLNITAGTME DMYERAEFAK ELGSCIVMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS
     TYTRQKSHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDVC REDFNPTKLE
     HGLFFDQSWA SLNKMMPVAS GGIHAGQMHQ LLDLLGEDVV LQFGGGTIGH PMGIAAGAIA
     NRVALEAMIL ARNEGRDYVH EGPEILAKAA QTCTPLKSAL EVWKDVTFNY QSTDTPDFVP
     TALETV
//
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