ID RBL2_HALNC Reviewed; 459 AA. AC Q9ZHZ4; D0KZQ8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339}; DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339}; DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339}; DE AltName: Full=Form II RuBisCO {ECO:0000303|PubMed:9696760}; GN Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339}; GN OrderedLocusNames=Hneap_1095; OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus OS neapolitanus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; OC Halothiobacillaceae; Halothiobacillus. OX NCBI_TaxID=555778; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Shively J.M.; RT "A form II Rubisco gene and associated genes in Thiobacillus RT neapolitanus."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23641 / c2; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Kerfeld C., Cannon G., Heinhort S.; RT "Complete sequence of Halothiobacillus neapolitanus c2."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP SUBCELLULAR LOCATION, AND INDUCTION. RC STRAIN=ATCC 23641 / c2; RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998; RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.; RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 RT requirement for growth."; RL J. Bacteriol. 180:4133-4139(1998). 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_01339}. 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_01339}; 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_01339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01339}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01339}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01339}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9696760}. CC -!- INDUCTION: Form II RuBisCO is expressed in the presence of form I, when CC grown in air with or without 5% CO(2), although it is not the major CC activity. When the form I gene is disrupted the RuBisCO form II CC activity increases, but is not found in carboxysomes (at protein CC level). {ECO:0000269|PubMed:9696760}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a 'head-to-tail' conformation. In contrast to form I CC RuBisCO, the form II RuBisCO are composed solely of large subunits. CC {ECO:0000255|HAMAP-Rule:MF_01339}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01339}. 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; AF046932; AAD02442.1; -; Genomic_DNA. DR EMBL; CP001801; ACX95931.1; -; Genomic_DNA. DR RefSeq; WP_012823967.1; NC_013422.1. DR AlphaFoldDB; Q9ZHZ4; -. DR SMR; Q9ZHZ4; -. DR STRING; 555778.Hneap_1095; -. DR KEGG; hna:Hneap_1095; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_6; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000009102; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 CDD; cd08211; RuBisCO_large_II; 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_01339; RuBisCO_L_type2; 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; IPR020871; RuBisCO_lsuII. 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 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 1: Evidence at protein level; KW Calvin cycle; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium; KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome. FT CHAIN 1..459 FT /note="Ribulose bisphosphate carboxylase" FT /id="PRO_0000062670" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT ACT_SITE 287 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 111 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 368 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT SITE 329 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT MOD_RES 191 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" SQ SEQUENCE 459 AA; 50573 MW; 84101EDB69A063FF CRC64; MDQSARYADL SLKEEDLIAG GKHILVAYKM KPKAGHGYLE ASAHFAAESS TGTNVEVSTT DDFTKGVDAL VYYIDEATED MRIAYPMDLF DRNVTDGRMM LVSVLTLIIG NNQGMGDIEH AKIHDIYFPE RAIQLFDGPS KDISDMWRIL GRPIENGGYI AGTIIKPKLG LRPEPFAAAA YQFWLGGDFI KNDEPQGNQV FCPLKKVLPL VYDSMKRAQD ETGQAKLFSM NITADDHYEM MARADFGLET FGPDADKLAF LVDGFVGGPG MITTARRQYP NQYLHYHRAG HGMITSPSAK RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGEGDDRNIA YMIERDEAQG PVYFQKWYGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGSYGHI DSPAAGAISL KQAYECWKAG ADPIEFAKEH KEFARAFESF PKDADAIFPG WREKLGVHK //