ID   RBLL_CHLTI              Reviewed;         434 AA.
AC   Q9AMC5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Ribulose bisphosphate carboxylase-like protein;
DE            Short=RuBisCO-like protein;
DE   Flags: Fragment;
OS   Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp.
OS   thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=115852;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK14332.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 249 / 6230 / Tassajara;
RX   PubMed=11287671; DOI=10.1073/pnas.081610398;
RA   Hanson T.E., Tabita F.R.;
RT   "A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein
RT   from Chlorobium tepidum that is involved with sulfur metabolism and the
RT   response to oxidative stress.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4397-4402(2001).
CC   -!- FUNCTION: May be involved in sulfur metabolism and oxidative stress
CC       response. Does not show RuBisCO activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q8KBL4}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8KBL4}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to RuBisCO family, it lacks the
CC       conserved Lys active site in position 327, which is replaced by an Arg
CC       residue, suggesting that it may catalyze enolization but not
CC       carboxylation. {ECO:0000305}.
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DR   EMBL; AF326322; AAK14332.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AMC5; -.
DR   SMR; Q9AMC5; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   InterPro; IPR033966; RuBisCO.
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; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding.
FT   CHAIN           1..>434
FT                   /note="Ribulose bisphosphate carboxylase-like protein"
FT                   /id="PRO_0000062680"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         198
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         434
FT                   /evidence="ECO:0000312|EMBL:AAK14332.1"
SQ   SEQUENCE   434 AA;  48033 MW;  3ABCF1327C4955F0 CRC64;
     MNAEDVKGFF ASRESLDMEQ YLVRDYYLEC VGDIETALAH FCSEQSTAQW KRVGVDEDFR
     PMHAAKVIDY DVIEELEQLS YPVKHSETGK IHACRVTIAH PHCNFGPKIP NLLTAVCGEG
     TYFTPGVPVV KLMDIHFPDI YLADFEGPKF GIDGLRNILN AHGRPIFFGV VKPNIGLSPE
     EFSEIAYQSW LGGLDIAKDD EMLADVTWSS IEERAAHLGK ARRKAEAETG EPKIYLANIT
     DEVDSLMEKH DIAVRNGANA LLINALPVGL SAVRMLSNYT QVPLIGHFPF IASFSRMEKY
     GIRSKVMTKL QRLAGLDVVI MPGFGDRMMT PEEEVVENVI ECTKPMGRIK PCLPVPGGSD
     SALTLGTVWR KVGSVDFGFV PGRGVFGHPM GPRAGAKSIR QAWEAIEQGI SIETWAETHP
     ELQAMIDQSA LKKQ