ID   B3QT65_CHLT3            Unreviewed;       433 AA.
AC   B3QT65;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Ribulose-bisphosphate carboxylase {ECO:0000313|EMBL:ACF14164.1};
DE            EC=4.1.1.39 {ECO:0000313|EMBL:ACF14164.1};
GN   OrderedLocusNames=Ctha_1707 {ECO:0000313|EMBL:ACF14164.1};
OS   Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC   Chloroherpeton.
OX   NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF14164.1, ECO:0000313|Proteomes:UP000001208};
RN   [1] {ECO:0000313|EMBL:ACF14164.1, ECO:0000313|Proteomes:UP000001208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; CP001100; ACF14164.1; -; Genomic_DNA.
DR   RefSeq; WP_012500248.1; NC_011026.1.
DR   AlphaFoldDB; B3QT65; -.
DR   STRING; 517418.Ctha_1707; -.
DR   KEGG; cts:Ctha_1707; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_10; -.
DR   OrthoDB; 9770811at2; -.
DR   Proteomes; UP000001208; Chromosome.
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   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; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ACF14164.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001208}.
FT   DOMAIN          34..141
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          151..429
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   433 AA;  48011 MW;  BB7568F5C58E0DD0 CRC64;
     MEAKDIPGFF AKPEEIDAEK YIYLDYYFEC IGEPEAAAAH LCSEQSTAQW KRVGIDEDFR
     EEFGAKVLEL KVIKELDEIS CPVKNVFDGK TYACKAKIAH PHNNFGPRIP NLLSAVCGEG
     TFFSPGIPII KLLDIHFPKS YLNQFEGPKF GIEGLREILN VYDRPIFFGV IKPNIGLPPE
     PFSEIGYQSW LGGLDIAKDD EMLADTSWSP TPIRSKLLGA AREKAERETG VPKIYLANIT
     DEVDRIIELH DIAVENGANA LMLNAMPVGL SAVRMLRKHT KVPLIAHFPF TASFSRMQHY
     GIHSQVITKL QRLAGFDSII MPGFGNRMMT PEDEVLQNIK ACYEDMGHIK RVLPVPGGSD
     SAVTLKNVYE KVGSTDFGFV PGRGVFGHPM GPKAGAASIR QAWEAISSAT PIETYAETHE
     ELKAAIHAFS KRK
//