ID Q12HJ3_POLSJ Unreviewed; 428 AA. AC Q12HJ3; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 91. DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit {ECO:0000313|EMBL:ABE41999.1}; DE EC=4.1.1.39 {ECO:0000313|EMBL:ABE41999.1}; GN OrderedLocusNames=Bpro_0032 {ECO:0000313|EMBL:ABE41999.1}; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE41999.1, ECO:0000313|Proteomes:UP000001983}; RN [1] {ECO:0000313|Proteomes:UP000001983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983}; RX PubMed=18723656; DOI=10.1128/AEM.00197-08; RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S., RA Stothard P., Coleman N.V.; RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of RT relevance to biotechnology."; RL Appl. Environ. Microbiol. 74:6405-6416(2008). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. CC {ECO:0000256|RuleBase:RU003834}. 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; CP000316; ABE41999.1; -; Genomic_DNA. DR RefSeq; WP_011481009.1; NC_007948.1. DR AlphaFoldDB; Q12HJ3; -. DR STRING; 296591.Bpro_0032; -. DR KEGG; pol:Bpro_0032; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_0_4; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000001983; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015977; P:carbon fixation; IEA:InterPro. DR CDD; cd08207; RLP_NonPhot; 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 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 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; 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 Lyase {ECO:0000313|EMBL:ABE41999.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000001983}. FT DOMAIN 17..133 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 143..426 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 428 AA; 45344 MW; F99E6684D661C770 CRC64; MNADRFEATY LIETPLEPAR VAEVMAGEQS CGTFTRVEGE TDALRLRARA TVESIEELAS VNAPSLPNAL LERQGHTAPH GGPWRRARVR ISFPVANVGA NLPTLAATVS GNLYDLGEAS GLRLESMKLP AAYRAQFDRP RVGIAGTRQA TGVASGALVG TILKPNVGFS AAQTAELVGR LCAAGVDFIK DDEVCADPAH APLAKRVPAV MAVVRAHQQR TGKHVMVAFN ITDETDAMKR HADLVEREGG SCVMASLNWC GHSALQTLRR HTGLALHGHR NGYGALSRHP LLGMSFQAYQ TLWRLAGVDH MHVHGLQGKF SQPDAEVIES AHDCYTPLAD GADGFDDRVM PAFSSGQWAG TVPATWAAVQ SDDLLFMSGG GILAHPGGPA AGVASIRQAW AAARQGVALA EFAREAPELA AALAFFGK //