ID   RBL1B_ACIF2             Reviewed;         473 AA.
AC   B7JA24; Q07087; Q9APC8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Name=cbbL2 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Synonyms=rbcL2 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=AFE_3051;
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Heinhorst S., Rugh D., Cannon G.C., Shively J.M.;
RT   "Thiobacillus ferrooxidans ATCC 23270, the type strain, possesses two sets
RT   of form I ribulose bisphosphate carboxylase/oxygenase (RuBisCO) genes and a
RT   form II RuBisCO gene.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(2008).
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:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CAUTION: In A.ferrooxidans two similar set of genes code for RuBisCO
CC       large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets.
CC       {ECO:0000305}.
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DR   EMBL; AF307091; AAK00291.1; -; Genomic_DNA.
DR   EMBL; CP001219; ACK80366.1; -; Genomic_DNA.
DR   RefSeq; WP_009566926.1; NC_011761.1.
DR   AlphaFoldDB; B7JA24; -.
DR   SMR; B7JA24; -.
DR   STRING; 243159.AFE_3051; -.
DR   PaxDb; 243159-AFE_3051; -.
DR   GeneID; 66433993; -.
DR   KEGG; afr:AFE_3051; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_2_0_6; -.
DR   Proteomes; UP000001362; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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_01338; RuBisCO_L_type1; 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; IPR020888; RuBisCO_lsuI.
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; SFLDG01052; RuBisCO; 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   Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..473
FT                   /note="Ribulose bisphosphate carboxylase large chain 2"
FT                   /id="PRO_0000369191"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            327
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         194
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   CONFLICT        400
FT                   /note="L -> I (in Ref. 1; AAK00291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  52702 MW;  D95289292292471A CRC64;
     MAVKTYNAGV KDYRNTYWEP DYSVKDTDIL AVFKITPQAG VDREEAAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
     KAVRALRLED VRFPIAYVKT CGGPPHGIQV ERDIMNKYGR PLLGCTIKPK LGLSAKNYGR
     ACYEGLRGGL DFTKDDENVN SQPFMRWRQR FDFVMEAIQK AEAETGERKG HYLNVTAPTP
     EEMYKRAEYA KEIGAPIIMH DYITGGFCAN TGLANWCRDN GMLLHIHRAM HAVLDRNPHH
     GIHFRVLTKI LRLSGGDHLH SGTVVGKLEG DREATLGWID IMRDRFIKED RSRGIFFDQD
     WGSMPGVMPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNRGVAI EKEGKAVLTE AAKHSPELKI AMETWKEIKF EFDTVDKLDV AHK
//