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Database: UniProt/TrEMBL
Entry: F8GEW5_NITSI
LinkDB: F8GEW5_NITSI
Original site: F8GEW5_NITSI 
ID   F8GEW5_NITSI            Unreviewed;       473 AA.
AC   F8GEW5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-SEP-2017, entry version 42.
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   OrderedLocusNames=Nit79A3_1255 {ECO:0000313|EMBL:AEJ01097.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01097.1, ECO:0000313|Proteomes:UP000000501};
RN   [1] {ECO:0000313|EMBL:AEJ01097.1, ECO:0000313|Proteomes:UP000000501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01097.1,
RC   ECO:0000313|Proteomes:UP000000501};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A.,
RA   Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D.,
RA   Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
CC       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; CP002876; AEJ01097.1; -; Genomic_DNA.
DR   RefSeq; WP_013965373.1; NC_015731.1.
DR   STRING; 261292.Nit79A3_1255; -.
DR   EnsemblBacteria; AEJ01097; AEJ01097; Nit79A3_1255.
DR   KEGG; nii:Nit79A3_1255; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   KO; K01601; -.
DR   OMA; EYRETYW; -.
DR   OrthoDB; POG091H14UZ; -.
DR   Proteomes; UP000000501; 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; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
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 {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000501};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338};
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:UP000000501}.
FT   DOMAIN       16    137       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      147    455       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    287    287       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       194    194       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       196    196       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       197    197       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     116    116       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     166    166       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     288    288       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     320    320       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     372    372       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        327    327       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     194    194       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   473 AA;  52459 MW;  23F07A35161E6884 CRC64;
     MAVKIYNAGV KEYRHTYWTP DYTPLDTDLL ACFKITPQAG VPREEVAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYKI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF
     KALRALRLED VRFPIAYVKT CGGPPAGIQV ERDRLNKYGR ALLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DLTKDDENVN SQPFMRWRDR FEFVVEACQK AERETGERKG HYLNVTAPTP
     EEMYKRAEFA KELGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH
     GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DRAATLGWID TMRDKFIKED RSRGLFFDQD
     WGSMPGVFPV ASGGIHVWHM PALVAIFGDD ACLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNQGVEI EKEGKAILTK AAKSSPELKI AMETWKEIKF EFDTVDKLDV AHK
//
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