ID E3HQ31_ACHXA Unreviewed; 425 AA. AC E3HQ31; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 61. DE SubName: Full=Ribulose bisphosphate carboxylase large chain, catalytic domain protein {ECO:0000313|EMBL:ADP17189.1}; DE EC=4.1.1.39 {ECO:0000313|EMBL:ADP17189.1}; GN OrderedLocusNames=AXYL_03869 {ECO:0000313|EMBL:ADP17189.1}; OS Achromobacter xylosoxidans (strain A8). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17189.1, ECO:0000313|Proteomes:UP000006876}; RN [1] {ECO:0000313|EMBL:ADP17189.1, ECO:0000313|Proteomes:UP000006876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A8 {ECO:0000313|EMBL:ADP17189.1, RC ECO:0000313|Proteomes:UP000006876}; RX PubMed=21097610; DOI=10.1128/JB.01299-10; RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.; RT "Complete genome sequence of the haloaromatic acids-degrading bacterium RT Achromobacter xylosoxidans A8."; RL J. Bacteriol. 193:791-792(2011). 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; CP002287; ADP17189.1; -; Genomic_DNA. DR RefSeq; WP_013394503.1; NC_014640.1. DR AlphaFoldDB; E3HQ31; -. DR STRING; 762376.AXYL_03869; -. DR KEGG; axy:AXYL_03869; -. DR PATRIC; fig|762376.5.peg.3884; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_0_4; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000006876; 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:ADP17189.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. FT DOMAIN 15..131 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 141..421 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 425 AA; 45591 MW; 45AFBF21D457815F CRC64; MNSQSFTATY LIETPLDPAK VAEVMAGEQS CGTFTRVQGE TDELRARARA RIESIETLES AAAPSLPNAW LARQPGGMPG LYRRARVRIA FPVANVGASL PTLAATVGGN LYDLGEVTGL RLESMELPAN YRAQFDVPRV GIAGTRQLTG VAHGPLVGTI IKPNVGLSPE QTAHLAAQLC AAGVDFIKDD EVCANPAHAP LAQRVAAVMA VVRAHRERTG RQVMVAFNIS DETDAMRRHA DLIEREGGTC VMASLNHCGY SAIQTLRRST PLALHGHRNG YGALSRHPLL GLGFQAYQTL WRLAGVDHMH VHGLQGKFSQ EDAEVVESAR DCLASLTLGI DDPVMPAFSS GQWAGTVPAT WAAVRSDDLL FMSGGGILAH PDGPAAGVLS IRQAWQAMRD GERLEDYARN APELRRAIEC FGHRA //