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Database: UniProt/SWISS-PROT
Entry: RBL_OLICO
LinkDB: RBL_OLICO
Original site: RBL_OLICO 
ID   RBL_OLICO               Reviewed;         486 AA.
AC   Q6LBA6; F8C111;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=OCA5_pHCG300470;
OS   Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145
OS   / OM5).
OG   Plasmid megaplasmid pHCG3.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Oligotropha.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MRNA EXPRESSION.
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=10433972; DOI=10.1016/S0378-1119(99)00245-0;
RA   Santiago B., Schuebel U., Egelseer C., Meyer O.;
RT   "Sequence analysis, characterization and CO-specific transcription of
RT   the cox gene cluster on the megaplasmid pHCG3 of Oligotropha
RT   carboxidovorans.";
RL   Gene 236:115-124(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=14644498; DOI=10.1016/j.gene.2003.08.027;
RA   Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
RT   "Complete nucleotide sequence of the circular megaplasmid pHCG3 of
RT   Oligotropha carboxidovorans: function in the chemolithoautotrophic
RT   utilization of CO, H(2) and CO(2).";
RL   Gene 322:67-75(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/JB.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
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:
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};
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   -!- 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   -!- INDUCTION: Expressed under CO(2) and H(2) autotrophic, but not
CC       under heterotrophic growth conditions.
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; CP002827; AEI08121.1; -; Genomic_DNA.
DR   RefSeq; WP_013913745.1; NC_015689.1.
DR   ProteinModelPortal; Q6LBA6; -.
DR   SMR; Q6LBA6; -.
DR   EnsemblBacteria; AEI08121; AEI08121; OCA5_pHCG300470.
DR   KEGG; ocg:OCA5_pHCG300470; -.
DR   PATRIC; fig|504832.7.peg.3622; -.
DR   KO; K01601; -.
DR   OMA; FTQDWAS; -.
DR   Proteomes; UP000007730; Plasmid pHCG3.
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   2: Evidence at transcript level;
KW   Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Plasmid;
KW   Reference proteome.
FT   CHAIN         1    486       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062635.
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}.
SQ   SEQUENCE   486 AA;  53763 MW;  B200320194573F67 CRC64;
     MNDQSMTIRG KDRYKSGVMA YKKMGYWEPD YVPKDTDVIA LFRVTPQDGV DPIEAAAAVA
     GESSTATWTV VWTDRLTAAE KYRAKCYRVD PVPNSPGQYF AYIAYDLDLF EPGSISNLTA
     SIIGNVFGFK PLKGLRLEDM RLPVAYVKTF QGPATGIVVE RERLDKFGRP LLGATVKPKL
     GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRERF LYCMEAVNRA QAASGEVKGT
     YLNVTAATME DMYERAEFAK ELGSCIVMID LVIGYTAIQS MAKWARKNDM ILHLHRAGHS
     TYTRQKNHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC REEFNPTKLE
     HGIFFDQNWA SLNKMMPVAS GGIHAGQMHQ LLDLLGEDVV LQFGGGTIGH PMGIQAGAIA
     NRVALEAMIL ARNEGRDYVA EGPEILAKAA ATCTPLKSAL EVWKDVTFNY ESTDAPDFVP
     TAIAAV
//
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