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Database: UniProt/TrEMBL
Entry: A0A0F7KDF3_9PROT
LinkDB: A0A0F7KDF3_9PROT
Original site: A0A0F7KDF3_9PROT 
ID   A0A0F7KDF3_9PROT        Unreviewed;       473 AA.
AC   A0A0F7KDF3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
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=rbcL {ECO:0000313|EMBL:AKH38550.1};
GN   Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
GN   ORFNames=AAW31_13310 {ECO:0000313|EMBL:AKH38550.1}, SAMN05421882_10579
GN   {ECO:0000313|EMBL:SDX08048.1};
OS   Nitrosomonas communis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH38550.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKH38550.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nm2 {ECO:0000313|EMBL:AKH38550.1};
RX   PubMed=26769932;
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic
RT   Ammonia-Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL   Genome Announc. 4:0-0(2016).
RN   [3] {ECO:0000313|EMBL:SDX08048.1, ECO:0000313|Proteomes:UP000183454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm110 {ECO:0000313|EMBL:SDX08048.1,
RC   ECO:0000313|Proteomes:UP000183454};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; CP011451; AKH38550.1; -; Genomic_DNA.
DR   EMBL; FNNH01000057; SDX08048.1; -; Genomic_DNA.
DR   RefSeq; WP_046850588.1; NZ_FNNH01000057.1.
DR   EnsemblBacteria; AKH38550; AKH38550; AAW31_13310.
DR   KEGG; nco:AAW31_13310; -.
DR   PATRIC; fig|44574.3.peg.3238; -.
DR   KO; K01601; -.
DR   Proteomes; UP000034156; Chromosome.
DR   Proteomes; UP000183454; Unassembled WGS sequence.
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; 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 {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034156,
KW   ECO:0000313|Proteomes:UP000183454};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:AKH38550.1};
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:UP000034156}.
FT   DOMAIN       16    136       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;  52719 MW;  1D86E65BC6E70AF0 CRC64;
     MAVKTYSAGV KEYRQTYWEP DYNVQDTDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYHI EDVPGDDTCF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
     KAIRALRLED VRFPIAFVKT CGGPPYGIQA ERDKLNKYGR ALLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DLTKDDENIN SQPFMRWRQR FEFVMEAIHK AERETGERKG HYLNVTAPTP
     EEMYKRAEFA KELGAPIIMH DYLTGGFTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH
     GIHFRVLAKA LRLSGGDHLH SGTVVGKLEG DREATLGWID IMRESFIKED RNRGIFFDQD
     WGSMPGVFPV ASGGIHVWHM PALVAIFGDD ACLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNEGIPI EKEGKAILTQ AAKHSPELKI AMETWKEIKF EFDTVDKLDV AHK
//
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