ID   F4CCC3_SPHS2            Unreviewed;       414 AA.
AC   F4CCC3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Ribulose-bisphosphate carboxylase {ECO:0000313|EMBL:ADZ78716.1};
DE            EC=4.1.1.39 {ECO:0000313|EMBL:ADZ78716.1};
GN   OrderedLocusNames=Sph21_2161 {ECO:0000313|EMBL:ADZ78716.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ78716.1};
RN   [1] {ECO:0000313|EMBL:ADZ78716.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ78716.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; CP002584; ADZ78716.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CCC3; -.
DR   STRING; 743722.Sph21_2161; -.
DR   KEGG; shg:Sph21_2161; -.
DR   PATRIC; fig|743722.3.peg.2308; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_0_10; -.
DR   OrthoDB; 9770811at2; -.
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; cd08207; RLP_NonPhot; 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   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; 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   Lyase {ECO:0000313|EMBL:ADZ78716.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          4..123
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          133..411
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   414 AA;  45385 MW;  15C9D63E71206BD1 CRC64;
     MERIIAKYYI ETPFDPEKAA LTLAGEQSSG TFVSVPGETE DLKRRFAARV ESVHLLGSVS
     QPAIPSPKFT SERYQRAYIE ISWSIENFGY NLPVLISTLQ GNLYELSQFT GLKLLDIQFP
     ASYIAHFEGP RFGVAGSRAS TKVDGRPLIG TIIKPSIGMS PSDSARLVKT LVEAGIDFIK
     DDELQSAAAN SKLEDRVDAI MRVINAHADK TGKKVMYAFN ISDELDSMLS RYDYIVKAGG
     TCAMLSINSV GLAGVKKICD QGALVIHGHR NGWGMLNRHP LLGIEFTAYQ KLWRLAGVDQ
     LHVNGIQNKF WESDDSVVQS IEACLTPLFS RETLLPVVSS GQWGGQAFET YRRTKTIDLL
     YMAGGGIMAH PKGPGGGVVA LQQAWEGAVK GLVMEEAVRL YPEFAQSVQK FGQQ
//