RBL_PSEUX
ID RBL_PSEUX Reviewed; 476 AA.
AC F4CQ77;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:23663433};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:23663433};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:23663433};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000303|PubMed:23663433};
GN OrderedLocusNames=Psed_6249;
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Pseudonocardia.
OX NCBI_TaxID=675635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190;
RX PubMed=21725009; DOI=10.1128/jb.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190;
RX PubMed=23663433; DOI=10.1111/1462-2920.12144;
RA Grostern A., Alvarez-Cohen L.;
RT "RubisCO-based CO2 fixation and C1 metabolism in the actinobacterium
RT Pseudonocardia dioxanivorans CB1190.";
RL Environ. Microbiol. 15:3040-3053(2013).
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:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000305|PubMed:23663433}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000305|PubMed:23663433};
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:0000255|HAMAP-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-Rule:MF_01338};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- INDUCTION: Transcription is 27-fold up-regulated by growth on
CC H(2)/bicarbonate compared to pyruvate, RuBisCO activity is induced by
CC growth on H(2), H(2)/bicarbonate, formate, methanol and CO.
CC {ECO:0000269|PubMed:23663433}.
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:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; CP002593; AEA28350.1; -; Genomic_DNA.
DR RefSeq; WP_013678237.1; NC_015312.1.
DR AlphaFoldDB; F4CQ77; -.
DR SMR; F4CQ77; -.
DR STRING; 675635.Psed_6249; -.
DR EnsemblBacteria; AEA28350; AEA28350; Psed_6249.
DR KEGG; pdx:Psed_6249; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_11; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000007809; 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-UniRule.
DR CDD; cd08212; RuBisCO_large_I; 1.
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 PANTHER; PTHR42704; PTHR42704; 1.
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 2: Evidence at transcript level;
KW Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..476
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000452045"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 116
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 326
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 194
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ SEQUENCE 476 AA; 52620 MW; 7CD92F1F43816FA0 CRC64;
MADRWNAGVI PYAEMGYWQP DYEPKDTDIL CAFRITPQDG VPPEEAGAAV AGESSTATWT
VVWTDRLTTF EHYQAKCYKV DPVPNTPGQW IAYIAYDIDL FEEASIANLT SSIIGNVFGF
KPLKALRLED MRIPTHYVKT FQGPAHGIVM EREHLGKFGR PILGATTKPK LGLSARNYGR
VVYEALRGGL DFTKDDENIN SQPFMRWRDR FLFCMEAVNR AQAATGEIKG HYLNVTAGTM
EEMYERANFA AELGSVIVMI DLTIGYTAIQ SMAKWARDNN VILHLHRAGH GTYTRQKNHG
VSFRVISKWM RLAGVDHIHA GTVVGKLEGD PMTTAGFYDT LRKDSIKADL SKGLYFDQEW
ASMPGVMPVA SGGIHAGQMH QLIHYLGEDV ILQFGGGTIG HPMGIAAGAE ANRVALEAMI
KARNEGVDYY KEGPEILKKA ASRNRALDTA LATWGDITFN YESTDTPDVV ATPTNA
