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Database: UniProt/SWISS-PROT
Entry: RBL_NITEU
LinkDB: RBL_NITEU
Original site: RBL_NITEU 
ID   RBL_NITEU               Reviewed;         473 AA.
AC   Q82TG6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-OCT-2017, entry version 93.
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   Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=NE1921;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 /
OS   NBRC 14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and
RT   obligate chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD85832.1; -; Genomic_DNA.
DR   RefSeq; WP_011112458.1; NC_004757.1.
DR   ProteinModelPortal; Q82TG6; -.
DR   SMR; Q82TG6; -.
DR   STRING; 228410.NE1921; -.
DR   PRIDE; Q82TG6; -.
DR   EnsemblBacteria; CAD85832; CAD85832; NE1921.
DR   KEGG; neu:NE1921; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; EYRETYW; -.
DR   OrthoDB; POG091H14UZ; -.
DR   PhylomeDB; Q82TG6; -.
DR   Proteomes; UP000001416; 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; 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   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; 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_0000062629.
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;  52799 MW;  911B9F731A66EE41 CRC64;
     MSAKTYNAGV KEYRHTYWEP HYNVQDTDIL ACFKIVPQPG VDREEAAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRSYRI EDVPGDDSSF YAFIAYPIDL FEEGSVVNVL TSLTGNVFGF
     KAVRSLRLED VRFPIAYVKT CGGPPNGIQV ERDILNKYGR AYLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENVN SQPFMRWRQR FDFVMEAIHK AERETGERKG HYLNVTAPTP
     EEMFKRAEYA KELKAPIIMH DYIAGGFCAN TGLANWCRDN GILLHIHRAM HAVIDRNPHH
     GIHFRVLAKM LRLSGGDHLH SGTVVGKLEG DREATLGWID IMRDSFIKED RSRGIMFDQD
     WGSMPGVVPV ASGGIHVWHM PALVTIFGDD ACLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNRGVPI EKEGKAILTE AAKHSPELKI AMETWKEIKF EFDTVDKLDV AHK
//
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