ID   L0H1D5_9GAMM            Unreviewed;       464 AA.
AC   L0H1D5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN   ORFNames=Thimo_3339 {ECO:0000313|EMBL:AGA92011.1};
OS   Thioflavicoccus mobilis 8321.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thioflavicoccus.
OX   NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA92011.1, ECO:0000313|Proteomes:UP000010816};
RN   [1] {ECO:0000313|EMBL:AGA92011.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8321 {ECO:0000313|EMBL:AGA92011.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA   Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site. {ECO:0000256|ARBA:ARBA00003617}.
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. Type II
CC       subfamily. {ECO:0000256|ARBA:ARBA00005475}.
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DR   EMBL; CP003051; AGA92011.1; -; Genomic_DNA.
DR   RefSeq; WP_015282139.1; NC_019940.1.
DR   AlphaFoldDB; L0H1D5; -.
DR   STRING; 765912.Thimo_3339; -.
DR   KEGG; tmb:Thimo_3339; -.
DR   PATRIC; fig|765912.4.peg.3272; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_6; -.
DR   OrthoDB; 9770811at2; -.
DR   Proteomes; UP000010816; 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   CDD; cd08211; RuBisCO_large_II; 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   HAMAP; MF_01339; RuBisCO_L_type2; 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   InterPro; IPR020871; RuBisCO_lsuII.
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:UP000010816}.
FT   DOMAIN          15..132
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          144..442
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   464 AA;  51119 MW;  2C871768CBC07A7B CRC64;
     MALDQSARYA DLSLKEIDLI DGGKHILCAY RMKPKGGYSY LEAAAHFAAE SSTGTNVEVC
     TTDDFTKGVD ALVYSIDEAR EEMRIAYPLD LFDRNMTDGR MMLVSFLTLT IGNNQGMGDI
     EYAKMIDFWM PPRAIQLFDG PSKNISDLWR ILGRPVQDGG YIAGTIIKPK LGLRPEPFAQ
     AAYQFWLGGD FIKNDEPQGN QTFAPVKKVM PLVYDAMKRA QDETGEAKLF SMNITADDHF
     EMCARADFAL ETFGSDADKL AFLVDGFVGG PGMVTTARRQ YPDQYLHYHR AGHGMITSPS
     SNRGYTAFVL AKMARLQGAS GIHVGTMGYG KMEGGADDRV IAYMIERDAC EGPVYYQEWY
     GMKPTTPIIS GGMNALRLPG FFQNLGHGNI INTAGGGSYG HLDSPAAGAK SLRQAYECWK
     SGADPIEFAK EHKEFARAFA SFPHDADKLF PGWREKLGSF ALEA
//