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Database: UniProt
Entry: W0P9J4_9BURK
LinkDB: W0P9J4_9BURK
Original site: W0P9J4_9BURK 
ID   W0P9J4_9BURK            Unreviewed;       495 AA.
AC   W0P9J4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-DEC-2018, entry version 28.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338};
GN   Name=cbbL {ECO:0000256|HAMAP-Rule:MF_01338,
GN   ECO:0000313|EMBL:AHG63529.1};
GN   ORFNames=MIM_c14380 {ECO:0000313|EMBL:AHG63529.1};
OS   Advenella mimigardefordensis DPN7.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1247726 {ECO:0000313|EMBL:AHG63529.1, ECO:0000313|Proteomes:UP000019095};
RN   [1] {ECO:0000313|EMBL:AHG63529.1, ECO:0000313|Proteomes:UP000019095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPN7 {ECO:0000313|EMBL:AHG63529.1,
RC   ECO:0000313|Proteomes:UP000019095};
RX   PubMed=24739217; DOI=10.1099/mic.0.078279-0;
RA   Wubbeler J.H., Hiessl S., Schuldes J., Thurmer A., Daniel R.,
RA   Steinbuchel A.;
RT   "Unravelling the complete genome sequence of Advenella
RT   mimigardefordensis strain DPN7T and novel insights in the catabolism
RT   of the xenobiotic polythioester precursor 3,3'-dithiodipropionate.";
RL   Microbiology 160:1401-1416(2014).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
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DR   EMBL; CP003915; AHG63529.1; -; Genomic_DNA.
DR   RefSeq; WP_025372163.1; NZ_CP003915.1.
DR   ProteinModelPortal; W0P9J4; -.
DR   EnsemblBacteria; AHG63529; AHG63529; MIM_c14380.
DR   KEGG; amim:MIM_c14380; -.
DR   PATRIC; fig|1247726.3.peg.1578; -.
DR   KO; K01601; -.
DR   Proteomes; UP000019095; 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   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019095};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:AHG63529.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019095}.
FT   DOMAIN       36    156       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      166    473       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    305    305       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       213    213       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       215    215       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       216    216       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     135    135       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     185    185       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     189    189       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     306    306       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     338    338       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     390    390       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        345    345       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     213    213       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   495 AA;  54754 MW;  CBA08FE8A787FC8C CRC64;
     MQGTQEIDNE RYQQRPDQGP KKRYAAGVLK YAQMGYWDGD YEPTDTDILA VFRITPQDGV
     DPIEAAAAVA GESSTATWTV VWTDRLTACD KYRAKAYRVD PVPNNEGQYF CYIAYDLSLF
     EEGSITNVTA SIIGNVFSFK PLKAARLEDM RFPAAYVKTF AGPPTGIIVE RERLDKFGRP
     LLGATTKPKL GLSGRNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LFVMDAVNKA
     SAATGEVKGS YLNITAGTME EMYRRAEFAK ELGSVIVMVD LVVGWTAIQS ISHWCRQNDM
     ILHMHRAGHG TYTRQKNHGV SFRVIAKWLR LAGVDHLHAG TAVGKLEGDP MTVQGYYNVC
     RDAYTQTDLP RGIFFDQDWV ALRKVLPVAS GGIHAGQMHQ LLELFGDDAI LQFGGGTIGH
     PDGIQAGAVA NRVALESMVL ARNEGRNIAE EGPQILKDAA KHCGPLRAAL DTWGEVTFNY
     QSTDTSDYTP VPSVA
//
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