ID   F7XHM6_SINMM            Unreviewed;       418 AA.
AC   F7XHM6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Ribulose bisphosphate carboxylaseoxygenase, large subunit protein {ECO:0000313|EMBL:AEH84052.1};
GN   Name=rbcL {ECO:0000313|EMBL:AEH84052.1};
GN   OrderedLocusNames=SM11_pD1220 {ECO:0000313|EMBL:AEH84052.1};
OS   Sinorhizobium meliloti (strain SM11).
OG   Plasmid pSmeSM11d {ECO:0000313|EMBL:AEH84052.1,
OG   ECO:0000313|Proteomes:UP000009045}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH84052.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH84052.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH84052.1,
RC   ECO:0000313|Proteomes:UP000009045};
RC   PLASMID=pSmeSM11d {ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(2011).
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; CP001832; AEH84052.1; -; Genomic_DNA.
DR   RefSeq; WP_010975267.1; NZ_JAJJBH010000002.1.
DR   AlphaFoldDB; F7XHM6; -.
DR   GeneID; 61600389; -.
DR   KEGG; smx:SM11_pD1220; -.
DR   PATRIC; fig|707241.3.peg.6906; -.
DR   HOGENOM; CLU_031450_3_0_5; -.
DR   Proteomes; UP000009045; Plasmid pSmeSM11d.
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   Plasmid {ECO:0000313|EMBL:AEH84052.1}.
FT   DOMAIN          13..121
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          131..412
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   418 AA;  44897 MW;  1757E4A35319E363 CRC64;
     MLRITYRIET PGDVEFLAKK IASDQSTGTF VPVPGETEEL KARVAARVLA IRHLEPADRA
     SWPDEAGSAT RFNRADAEIA FPLDAVGTDL SALMTIAIGG VYSIKGMTGI RIVDMKLPPE
     FAAAHPGPQF GVVGSRRLTG VEGRPIIGTI VKPALGLRPE ETAVLVGELL SSGVDFIKDD
     EKLMSPAYSP LSARIAAIMP RILDHEQKTG KKVMYAFGIS HTDPDEMMRN HDLVVAAGGN
     AAVVNINSVG MGGVAFLRKR SGLVLHAHRN GWDILTRHGG LGMEFSVWQQ FWRLLGVDQF
     QINGIRVKYW EPDESFVKSF EAVSTPLFTK DDCPLPVVGS GQWGGQAPET YARTGHTTDL
     LYLCGGGIVS HPGGPGAGVR AVRQAWEAAV AGIPLADYAR DHPELAQSLE KFADGKGA
//