ID B9KVC3_CERSK Unreviewed; 418 AA. AC B9KVC3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 74. DE SubName: Full=Ribulose bisphosphate carboxylaseoxygenase,large subunit {ECO:0000313|EMBL:ACM04001.1}; GN OrderedLocusNames=RSKD131_4141 {ECO:0000313|EMBL:ACM04001.1}; OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=557760 {ECO:0000313|EMBL:ACM04001.1, ECO:0000313|Proteomes:UP000001597}; RN [1] {ECO:0000313|EMBL:ACM04001.1, ECO:0000313|Proteomes:UP000001597} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD131 / KCTC 12085 {ECO:0000313|Proteomes:UP000001597}; RX PubMed=19028901; DOI=10.1128/JB.01565-08; RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.; RT "Complete genome sequence of Rhodobacter sphaeroides KD131."; RL J. Bacteriol. 191:1118-1119(2009). 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; CP001151; ACM04001.1; -; Genomic_DNA. DR RefSeq; WP_009566104.1; NC_011958.1. DR AlphaFoldDB; B9KVC3; -. DR GeneID; 67449392; -. DR KEGG; rsk:RSKD131_4141; -. DR HOGENOM; CLU_031450_3_0_5; -. DR Proteomes; UP000001597; Chromosome 2. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro. 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; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. FT DOMAIN 13..124 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 137..414 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 418 AA; 44575 MW; 39DC86D647A5E695 CRC64; MIRASYIVET PCPIAEVAAM MAGEQSAGTF VRVEGETDAL RARFGARVVE TAEIGRSERP SLRSAWAERR GLTGPRGLYR VVIDYPEENV GVNLPTLAAV VAGNLYDLGE VTGLKLMDVT LDPAYRARYE SPAMALAGTR ASLGVPSRPI FGTIIKPNIG LDPDEIAALV ARLCEAGADF IKDDEIAGTH PHAPVDARIR AVMREVRRHR DRTGRLVMVA FNISDETDAM RRHADLIAAE EGSCAMVSLN WCGLGAVQTL RRHTGLAIHG HRNGFGGMGR HPLLGMGVQA YQTLYRLAGI DHMHVHGMGG KFSDLDEDVA EAARHCLTGL GPADDRVMPV FSSGQWAGTL PHTLAETRSD ELMFLCGGGI MAHPGGPAAG LASLRQAHDA VRAGLDLAEA ARDRPELAAA LAAFGSGR //