ID   RBLL_ARCFU              Reviewed;         437 AA.
AC   O28685;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Ribulose bisphosphate carboxylase-like protein;
DE            Short=RuBisCO-like protein;
GN   OrderedLocusNames=AF_1587;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   FUNCTION.
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). {ECO:0000250,
CC       ECO:0000269|PubMed:11287671}.
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}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89661.1; -; Genomic_DNA.
DR   PIR; B69448; B69448.
DR   RefSeq; WP_010879084.1; NC_000917.1.
DR   AlphaFoldDB; O28685; -.
DR   SMR; O28685; -.
DR   STRING; 224325.AF_1587; -.
DR   DNASU; 1484815; -.
DR   EnsemblBacteria; AAB89661; AAB89661; AF_1587.
DR   GeneID; 1484815; -.
DR   KEGG; afu:AF_1587; -.
DR   eggNOG; arCOG04443; Archaea.
DR   HOGENOM; CLU_031450_3_1_2; -.
DR   OMA; AHFPFIA; -.
DR   PhylomeDB; O28685; -.
DR   Proteomes; UP000002199; Chromosome.
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; Reference proteome.
FT   CHAIN           1..437
FT                   /note="Ribulose bisphosphate carboxylase-like protein"
FT                   /id="PRO_0000062686"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         202
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  48560 MW;  B7C9D8AD01D078B5 CRC64;
     MQLGVRLRFQ KFEYPEANPE ALPEGIDPEE YIIGTYYMSF PKGMNPFEIT QVLALEQSTG
     TWLPVPGETP EVRRKHVAKV VGVYEIPDYE IMVPQEVDWR NFIVQIAFPW RNIGSKLSML
     FSTVVGNISM APKLKLLDLR FPKEFVKGFK GPKFGIEGVR DVLGVKDRPL LNNMIKPDVY
     SPPDLGAKLA YEVARGGVDI IKDDELLANP EFNRIEERVP KFMEAIDRAD EEKGEKTLYA
     VNVTADLPEV LENAERAIEL GANCLLVNYL ATGFPVLRAL AEDESIKVPI MAHMDVAGAY
     YVSPISGVRS TLILGKLPRL AGADIVVYPA PYGKAPMMEE KYIEVAKQHR YPFYHIKPCF
     PMPSGGIAPI MVPKLVNTLG KDFVVAAGGG IHAHPDGPAA GARAFRQAID AAMQGYTDLR
     KYAEENNLQE LLKALQL