ID A1AWY1_RUTMC Unreviewed; 460 AA.
AC A1AWY1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN OrderedLocusNames=Rmag_0701 {ECO:0000313|EMBL:ABL02438.1};
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthturnera.
OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL02438.1, ECO:0000313|Proteomes:UP000002587};
RN [1] {ECO:0000313|EMBL:ABL02438.1, ECO:0000313|Proteomes:UP000002587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm {ECO:0000313|EMBL:ABL02438.1};
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate. Both reactions occur simultaneously and in competition at
CC the same active site. {ECO:0000256|ARBA:ARBA00003617}.
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. Type II
CC subfamily. {ECO:0000256|ARBA:ARBA00005475}.
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DR EMBL; CP000488; ABL02438.1; -; Genomic_DNA.
DR RefSeq; WP_011738063.1; NC_008610.1.
DR AlphaFoldDB; A1AWY1; -.
DR STRING; 413404.Rmag_0701; -.
DR KEGG; rma:Rmag_0701; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_6; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000002587; 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; cd08211; RuBisCO_large_II; 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 InterPro; IPR020871; RuBisCO_lsuII.
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 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:ABL02438.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 14..130
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 144..441
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 460 AA; 50661 MW; 58A4E141FF56B3E6 CRC64;
MDQSNRYADL LLDEETLIKE GNHFLVAYTM TPMPGFGGYL ETAAHFAAES STGTNVEVST
TDDFTKDLDA MVYEIDEAKG TMKIAYPNNL FDRNLIDGRA MVVSLLTLII GNNQGMGDVQ
CAQIQDFWIS RKFLEIFDGP SLDITDLWSI LGRSRTDGGY IAGTIIKPKL GLRPKPFSEA
AYQFWLGGDF IKNDEPQGNQ VYARMKDVTP LVADAMRRAQ DETSEAKIFS ANITADDHHE
MCARADYILE TFAENAHHVA FLVDGYVGGC GMITTARRNY PNQYLHYHRA GHGAITSPSS
VRGYTAFVLG KLSRLMGASG IHVGTMGYGK MEGGADDRNI AYMIERDSAD GPVYHQEWFG
MKPTTPIISG GMNALRLPGF FENLGHGNVI NTSGGGSYGH IDSPAAGAKS LRQAYDCWMA
KADPIEFAKD HNEFARAFES FPNDADSLYP GWRDKLGIHK
//
