ID H6QYF8_NOCCG Unreviewed; 480 AA. AC H6QYF8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAR-2024, entry version 60. 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 ECO:0000313|EMBL:CCF64008.1}; GN OrderedLocusNames=NOCYR_3243 {ECO:0000313|EMBL:CCF64008.1}; OS Nocardia cyriacigeorgica (strain GUH-2). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Nocardia. OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF64008.1, ECO:0000313|Proteomes:UP000008190}; RN [1] {ECO:0000313|EMBL:CCF64008.1, ECO:0000313|Proteomes:UP000008190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF64008.1, RC ECO:0000313|Proteomes:UP000008190}; RX PubMed=22461543; DOI=10.1128/JB.00161-12; RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L., RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S., RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V., RA Richard Y., Cournoyer B., Blaha D.; RT "Genome sequence of the human- and animal-pathogenic strain Nocardia RT cyriacigeorgica GUH-2."; RL J. Bacteriol. 194:2098-2099(2012). 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; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; FO082843; CCF64008.1; -; Genomic_DNA. DR AlphaFoldDB; H6QYF8; -. DR STRING; 1127134.NOCYR_3243; -. DR KEGG; ncy:NOCYR_3243; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_2_0_11; -. DR Proteomes; UP000008190; 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; 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:UP000008190}. FT DOMAIN 22..142 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 154..459 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 173 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 291 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 121 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 175 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 199 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 201 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 202 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 292 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 324 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 376 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 331 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 199 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 480 AA; 52784 MW; 7E0BB1F29C3D6323 CRC64; MAEETVRDRW DPGVQSYASM GYYAPDYQPS DTDVLAVFRV TPQPGVDPIE AAAAVAGESS TATWTVVWTD RLTAHSKYQA KCYRIDEVPG RPGEYFAYVA YDLDLFEEGS ITNLTSSVIG NVFGFKPLLA LRLEDMRIPV AYVKTFQGPP HGTVMEREYL NKYGRALLGA TVKPKLGLSA RNYGRVVYEA CKGGLDFTKD DENINSQPFM RWRDRYLFAM EGVNRAMAET GEIKGHYLNV TAATMEQMYE RAEFAKELGS VVIMMDLTVG YTAMQSMSHW ARRNGVLLHL HRAGHSTFTR QKTHGVSFRV LAKWCRLIGV DHLHAGTVVG KLEGDPATTK GFYDTLRENV IATEPANGIF FDQHWASLPG VMPVASGGIH AGQMHQLVEL FGDDVILQFG GGTIGHPLGI AAGAEANRVA LEAIVQARNE GRDLLREGPE VLRKAAAVNR PLDVALATWG EVSFDYTSTD APDAVPTATH //