ID Q12HD2_POLSJ Unreviewed; 413 AA.
AC Q12HD2;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit {ECO:0000313|EMBL:ABE42060.1};
DE EC=4.1.1.39 {ECO:0000313|EMBL:ABE42060.1};
GN OrderedLocusNames=Bpro_0093 {ECO:0000313|EMBL:ABE42060.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE42060.1, 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}.
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DR EMBL; CP000316; ABE42060.1; -; Genomic_DNA.
DR RefSeq; WP_011481070.1; NC_007948.1.
DR AlphaFoldDB; Q12HD2; -.
DR STRING; 296591.Bpro_0093; -.
DR KEGG; pol:Bpro_0093; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_0_4; -.
DR OMA; AHFPFIA; -.
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:ABE42060.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 13..123
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 133..413
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 413 AA; 44240 MW; 6129481E62DAE443 CRC64;
MSERIHATYW LETGDDPRRA AEVIAGEQSS GTFITLPNET PALKARSGAR IERLEVLEQV
GQPSLPVATP AKVYTRCTLE LSWPIENLGP SLPNLMSTIA GNLFELRQVS GLRVLDLKLP
ASFAAAYPGP AFGIAGTRRL SGVAQGPLIG TIIKPSVGLD PAQTAEQVRQ LIDGGIDFIK
DDELQADGPH CPFDERVRAV MQVVNDAAQR DGRKVMVAFN LTGDLDQMRR RHDLVQSLGG
TCVMASLNSI GLVGLLELRR HASLPIHAHR CGWGYLSRSP ALGWDFAPWH QIWRLAGADH
LHVNGLANKF SESDASVIAA ARAVLRPLFA HQPMPAMPVF SSGQTGLQAP GTYAALGSAD
LIHAAGGGIF GHPGGIASGV SAFRQAWEAA MAGTPLHEHA KTHAELRSAL EFW
//