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Database: UniProt/SWISS-PROT
Entry: RBL_NITEC
LinkDB: RBL_NITEC
Original site: RBL_NITEC 
ID   RBL_NITEC               Reviewed;         473 AA.
AC   Q0AHW1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-OCT-2017, entry version 76.
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=Neut_0804;
OS   Nitrosomonas eutropha (strain C91).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C91;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M.,
RA   Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium,
RT   Nitrosomonas eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59071.1; -; Genomic_DNA.
DR   RefSeq; WP_011633896.1; NC_008344.1.
DR   ProteinModelPortal; Q0AHW1; -.
DR   SMR; Q0AHW1; -.
DR   STRING; 335283.Neut_0804; -.
DR   PRIDE; Q0AHW1; -.
DR   EnsemblBacteria; ABI59071; ABI59071; Neut_0804.
DR   KEGG; net:Neut_0804; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; EYRETYW; -.
DR   OrthoDB; POG091H14UZ; -.
DR   Proteomes; UP000001966; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
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; 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   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.
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    473       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000299966.
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;  52688 MW;  0E1D9FEAF68426BC CRC64;
     MAIKTYQAGV KEYRQTYWQP DYVPLDTDIL ACFKITPQSG VDREEAAAAV AAESSCGTWT
     TVWTDLLTDL DYYKGRAYRI EDVPGDDARF YAFVAYPIDL FEEGSVVNVF TSLVGNVFGF
     KAIRALRLED VRFPIAYVKT CGGPPSGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR
     AVYECLRGSL DFTKDDENIN SQPFMRWRDR FEFVQEATLK AEAETGERKG HYLNVTAPTP
     EEMYKRAEFA KEIGAPIIMH DYLAGGLCAN AGLANWCRNN GMLLHVHRAM HAVLDRNPHH
     GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFVPED RSRGIFFDQD
     WGSMPGAFAV ASGGIHVWHM PALVAIFGDD SVLQFGGGTL GHPWGNAAGA HANRVALEAC
     VQARNEGRQI EKEGREILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDI AHK
//
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