ID   L0FXC5_ECHVK            Unreviewed;       414 AA.
AC   L0FXC5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Ribulose 1,5-bisphosphate carboxylase, large subunit {ECO:0000313|EMBL:AGA77957.1};
GN   OrderedLocusNames=Echvi_1692 {ECO:0000313|EMBL:AGA77957.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA77957.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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; CP003346; AGA77957.1; -; Genomic_DNA.
DR   RefSeq; WP_015265519.1; NC_019904.1.
DR   AlphaFoldDB; L0FXC5; -.
DR   STRING; 926556.Echvi_1692; -.
DR   KEGG; evi:Echvi_1692; -.
DR   PATRIC; fig|926556.3.peg.1797; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_0_10; -.
DR   OrthoDB; 9770811at2; -.
DR   Proteomes; UP000010796; 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   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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010796}.
FT   DOMAIN          7..123
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          133..410
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   414 AA;  45086 MW;  2184B5344EA954A4 CRC64;
     MERISATYYI ETPFEVESAA AVLAGEQSSG TFVAVPGETA ELKQRFAARV ESIEKLETVS
     QPAIPGAVSS HGKYHRAMIS VSWSIENFGY NLPTMISTLQ GNLYEITQFT GLKLMDLEVP
     ASFAQHFAGP AFGIKGCREL TGVEAGRPLI GTIIKPSIGM RPEETAALVK TLVEAGIDFI
     KDDELMGSAA NSPFDKRVEA IMRVINAHAD KSGKKVMYAF NISDEMDRMH EHYDTVVKHG
     GTCAMMSINS VGMAGVKRIC DRRELAIHAH RNGWGMLNRH PLLGIDFRAY QKLWRLAGVD
     QLHVNGIQNK FWESDDSVVR SIAGCLTPML GGYQVLPVVS SGQWGGQAPE TYRRTETTDL
     LYMAGGGIMA HPAGPAGGVK ALQQAWRAAV DGLSVEEAAK KYEEFGLSVQ KFGK
//