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Database: UniProt
Entry: A0A0Q4ISF4_9SPHN
LinkDB: A0A0Q4ISF4_9SPHN
Original site: A0A0Q4ISF4_9SPHN 
ID   A0A0Q4ISF4_9SPHN        Unreviewed;       421 AA.
AC   A0A0Q4ISF4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Ribulose 1,5-bisphosphate carboxylase {ECO:0000313|EMBL:KQN05152.1};
GN   ORFNames=ASE85_20650 {ECO:0000313|EMBL:KQN05152.1};
OS   Sphingobium sp. Leaf26.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1735693 {ECO:0000313|EMBL:KQN05152.1, ECO:0000313|Proteomes:UP000051336};
RN   [1] {ECO:0000313|Proteomes:UP000051336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQN05152.1}.
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DR   EMBL; LMKV01000011; KQN05152.1; -; Genomic_DNA.
DR   RefSeq; WP_056686873.1; NZ_LMKV01000011.1.
DR   AlphaFoldDB; A0A0Q4ISF4; -.
DR   STRING; 1735693.ASE85_20650; -.
DR   OrthoDB; 9764279at2; -.
DR   Proteomes; UP000051336; Unassembled WGS sequence.
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}.
FT   DOMAIN          5..128
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          138..419
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   421 AA;  44535 MW;  3FE0A64B1A599403 CRC64;
     MSDRVFATYE IETAFPLAQA AATMAGEQST GTFVRVPGET DELREAHAAR VEVLDELGEV
     DAPSLPGSGL PKGGGDGKRR RARVTLSWPT SNFGISLPNL LATINGNLSE LKAFSGLRLV
     DVALPPAFLT RYQGPQFGVA GTRKLAGVHD RPMIGTIIKP SVGLSPEATA DQVRGLVEAG
     VDFIKDDELQ ADGPHCPFDA RVSAVMRVIN DHADRTGKKV MFAANLTGDM DEMLERHDHV
     LREGGTCIMA SMNSIGLPAM KMLRAHSQLP IHGHRNGWGM LGRSPAIGMS YIAFQKLWRL
     AGIDHTHVNG IDNKFCESNE SVIASARECL MPMFPSPHAG CEIMPVFSSG QSARQVPATF
     AALGSTDLIF AAGGGIMAHP GGPGAGVRAL QQAWAAAVAG VDLAEAATQE PELRDALAAF
     A
//
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