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Database: UniProt
Entry: RBL1_THIDA
LinkDB: RBL1_THIDA
Original site: RBL1_THIDA 
ID   RBL1_THIDA              Reviewed;         473 AA.
AC   Q56259; Q3SFM9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   10-OCT-2018, entry version 115.
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}; Synonyms=cbbL1;
GN   OrderedLocusNames=Tbd_2624;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], KINETIC PARAMETERS, FUNCTION, AND
RP   SUBUNIT.
RX   PubMed=8550452; DOI=10.1128/jb.178.2.347-356.1996;
RA   Hernandez J.M., Baker S.H., Lorbach S.C., Shively J.M., Tabita F.R.;
RT   "Deduced amino acid sequence, functional expression, and unique
RT   enzymatic properties of the form I and form II ribulose bisphosphate
RT   carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus
RT   denitrificans.";
RL   J. Bacteriol. 178:347-356(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic,
RT   facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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       ECO:0000269|PubMed:8550452}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=43 uM for ribulose 1,5-bisphosphate
CC         {ECO:0000269|PubMed:8550452};
CC         KM=138 uM for CO(2) {ECO:0000269|PubMed:8550452};
CC         KM=1637 uM for O(2) {ECO:0000269|PubMed:8550452};
CC         Vmax=1.8 umol/min/mg enzyme with CO(2) as substrate
CC         {ECO:0000269|PubMed:8550452};
CC         Vmax=0.5 umol/min/mg enzyme with O(2) as substrate
CC         {ECO:0000269|PubMed:8550452};
CC         Note=The CO(2)/O(2) specificity factor (tau) is 46.;
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains
CC       (By similarity). In R.sphaeroides the complex is approximately 500
CC       kDa. {ECO:0000255|HAMAP-Rule:MF_01338,
CC       ECO:0000269|PubMed:8550452}.
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; L42940; AAB70697.1; -; Genomic_DNA.
DR   EMBL; CP000116; AAZ98577.1; -; Genomic_DNA.
DR   RefSeq; WP_011313136.1; NC_007404.1.
DR   ProteinModelPortal; Q56259; -.
DR   SMR; Q56259; -.
DR   STRING; 292415.Tbd_2624; -.
DR   EnsemblBacteria; AAZ98577; AAZ98577; Tbd_2624.
DR   KEGG; tbd:Tbd_2624; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; EYRETYW; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; TDEN292415:G1G56-2650-MONOMER; -.
DR   Proteomes; UP000008291; 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   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    473       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062656.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    287    287       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       194    194       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       196    196       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       197    197       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     116    116       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     166    166       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     170    170       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     288    288       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     320    320       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     372    372       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        327    327       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     194    194       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   473 AA;  52694 MW;  470DC11519D580A7 CRC64;
     MAVKTYSAGV KEYRQTYWMP EYTPLDTDIL ACFKITPQAG VDREEAAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYAI EDVPGDDTCF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
     KAVRALRLED VRFPIAYVKT CGGPPHGIQV ERDVMNKYGR PLLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENVN SQPFMRWRQR FDFVMEAIQK SERETGERKG HYLNVTAPTP
     EEMYKRAEYA KEIGAPIIMH DYITGGFCAN TGLANWCRDN GMLLHIHRAM HAVLDRNPHH
     GIHFRVLTKI LRLSGGDHLH SGTVVGKLEG DREATLGWID MMRDSFVKED RSRGIFFDQD
     WGSMPGVFPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNKGVAI EKEGKTVLTE AAKNSPELKI AMETWKEIKF EFDTVDKLDV AHK
//
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