ID Q12HJ3_POLSJ Unreviewed; 428 AA.
AC Q12HJ3;
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: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}.
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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 OMA; IHGHPDG; -.
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
//