ID Q3B5T1_CHLL3 Unreviewed; 442 AA. AC Q3B5T1; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 92. DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit {ECO:0000313|EMBL:ABB23300.1}; DE EC=4.1.1.39 {ECO:0000313|EMBL:ABB23300.1}; GN OrderedLocusNames=Plut_0412 {ECO:0000313|EMBL:ABB23300.1}; OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon OS luteolum). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=319225 {ECO:0000313|EMBL:ABB23300.1, ECO:0000313|Proteomes:UP000002709}; RN [1] {ECO:0000313|Proteomes:UP000002709} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 273 / BCRC 81028 / 2530 RC {ECO:0000313|Proteomes:UP000002709}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelodictyon luteolum DSM 273."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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; CP000096; ABB23300.1; -; Genomic_DNA. DR AlphaFoldDB; Q3B5T1; -. DR STRING; 319225.Plut_0412; -. DR KEGG; plt:Plut_0412; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_10; -. DR Proteomes; UP000002709; 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 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; 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. PE 3: Inferred from homology; KW Lyase {ECO:0000313|EMBL:ABB23300.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002709}. FT DOMAIN 42..150 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 160..432 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 442 AA; 48660 MW; B711ED9A8457BC33 CRC64; MREGDEALLM NTDDIRGFFA SREQLDMADY LTLEYYVECV GDIETALAHF CSEQSTAQWR RVGHDEDFRP RFGAKVIGLQ IEGELEQLSY PVQHSETGPI HACRVTIAHP HRNFGPKLPN LLTAVCGEGV FFTPGIPVVK LLDITFPEPY LNAFDGPKFG IEGIRDLLKA YDRPIFFGVV KPNIGLSPAH FAEIAMESWL GGLDIAKDDE MLADVEWSTL AERSRELGLA RIRAEKETGE PKVYLANITD EVGSLKEQHD VAVRNGANAL LINALPVGLS AVRMLAAYTK VPLIGHFPFI AAFSRMEKYG IHSRVMTKLQ RLAGLDSIIM PGFGSRMMTP EEEVKENIAE CLQDFGHIRR SLPVPGGSDS ALTLETVYRK VGSVDFGFVP GRGIFGHPMG PKAGAASIRQ AWDAIEKGVS LERYAEGHPE LGAMVAGARR SH //