ID   G0JPS3_9PROT            Unreviewed;       459 AA.
AC   G0JPS3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN   ORFNames=Acife_1242 {ECO:0000313|EMBL:AEM47398.1};
OS   Acidithiobacillus ferrivorans SS3.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM47398.1, ECO:0000313|Proteomes:UP000009220};
RN   [1] {ECO:0000313|EMBL:AEM47398.1, ECO:0000313|Proteomes:UP000009220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3 {ECO:0000313|EMBL:AEM47398.1,
RC   ECO:0000313|Proteomes:UP000009220};
RX   PubMed=21705598; DOI=10.1128/JB.05373-11;
RA   Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT   "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT   ferrivorans SS3.";
RL   J. Bacteriol. 193:4304-4305(2011).
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; CP002985; AEM47398.1; -; Genomic_DNA.
DR   RefSeq; WP_014028655.1; NC_015942.1.
DR   AlphaFoldDB; G0JPS3; -.
DR   SMR; G0JPS3; -.
DR   STRING; 743299.Acife_1242; -.
DR   KEGG; afi:Acife_1242; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_6; -.
DR   Proteomes; UP000009220; 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   HAMAP; MF_01339; RuBisCO_L_type2; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009220}.
FT   DOMAIN          13..130
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          143..440
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   459 AA;  50246 MW;  01DA54B22D6CD319 CRC64;
     MDQSNRYADL SLRENDLISN GKHILVAYKM KPKAGHGYLE AAAHFAAESS TGTNVEVSTT
     DDFTKGVDAL VYHIDEAADD MRIAYPLELF DRNVTDGRMM IVSFLTLVIG NNQGMGDIEH
     GQMIDFFMPP RAIQLFDGPA KDISDLWRIL GRPVQNGGYI AGTIIKPKLG LRPEPFAAAA
     YQFWLGGDFI KNDEPQGNQV FAPVKKTIPL VYDAMKRAMD ETGAAKLFSM NITADDHYEM
     CARADFALET FGPDADKLAF LVDGFVGGPG MITTARRQYP GQYLHYHRAG HGMITSPSAN
     RGYTAFVLAK MARLQGASGI HVGTMGYGKM EGGADDRNIA YMIERDSCDG PVYHQEWYGM
     KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGAYGHI DSPAAGAVSL RQAYECWKAG
     ADPIAYAREH QEFARAFESF PGDADKLYPG WREKLGVHK
//