GenomeNet

Database: UniProt
Entry: A0A0B8NED2_9NOCA
LinkDB: A0A0B8NED2_9NOCA
Original site: A0A0B8NED2_9NOCA 
ID   A0A0B8NED2_9NOCA        Unreviewed;       482 AA.
AC   A0A0B8NED2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=NS07_v2contig00139-0010 {ECO:0000313|EMBL:GAM50140.1};
OS   Nocardia seriolae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM50140.1, ECO:0000313|Proteomes:UP000019401};
RN   [1] {ECO:0000313|EMBL:GAM50140.1, ECO:0000313|Proteomes:UP000019401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N-2927 {ECO:0000313|EMBL:GAM50140.1,
RC   ECO:0000313|Proteomes:UP000019401};
RA   Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA   Oshima S.;
RT   "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT   Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT   quinqueradiata) in Kochi Prefecture, Japan.";
RL   Genome Announc. 3:e00082-15(2015).
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 at
CC       the same active site. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00001067, ECO:0000256|HAMAP-
CC         Rule:MF_01338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000256|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-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 RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAM50140.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BAWD02000139; GAM50140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B8NED2; -.
DR   STRING; 37332.NS506_04565; -.
DR   Proteomes; UP000019401; 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-UniRule.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDG01052; RuBisCO; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_01338};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_01338};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01338};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW   Rule:MF_01338};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01338}; Reference proteome {ECO:0000313|Proteomes:UP000019401}.
FT   DOMAIN          24..144
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          154..461
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   SITE            333
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT   MOD_RES         201
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
SQ   SEQUENCE   482 AA;  53216 MW;  67D3CE04CC0EEC35 CRC64;
     MAGSADDQRG RWDPGVQSYA SMGYYAPDYQ PKDTDVLAVF RVTPQQGVDP VEASAAVAGE
     SSTATWTVVW TDRLTAHDRY QGKCYRVDEV PGRKGEYFAY VAYDLDLFEE GSITNLTSSV
     IGNVFGFKPL QALRLEDMRI PVAYVKTFQG PPHGIVMERE YLNKYGRPLL GATVKPKLGL
     SARNYGRVVY EACKGGLDFT KDDENINSQP FMRWRDRFLF AMEGVNRAIA ETGEMKGHYL
     HVTAGTMEDM YERAEFAKSL GSIIVMIDLT IGYTAMQSMS KWARRNGMLL HLHRAGHSTF
     TRQKTHGVSF RVLAKWCRLI GVDHLHAGTV IGKLEGDPHT VRGFYDTLRD NHIPLNPVNG
     IFFDQDWASL PGVMPLASGG IHAGQMHQLL DLFGDDAILQ FGGGTIGHPM GIAAGAEANR
     VALEAVVKAR NEGRDLLKEG PDVLRRTAAN CRPLDVALTT WGDVTFDYTS TDAPDAVPTA
     TR
//
DBGET integrated database retrieval system