ID Q9LBG7_9PROT Unreviewed; 109 AA.
AC Q9LBG7;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 03-MAY-2023, entry version 60.
DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase form II large subunit {ECO:0000313|EMBL:BAA94450.1};
DE Flags: Fragment;
GN Name=cbbM {ECO:0000313|EMBL:BAA94450.1};
OS uncultured deep-sea autotrophic bacterium ORII-8.
OC Bacteria; Pseudomonadota; environmental samples.
OX NCBI_TaxID=120181 {ECO:0000313|EMBL:BAA94450.1};
RN [1] {ECO:0000313|EMBL:BAA94450.1}
RP NUCLEOTIDE SEQUENCE.
RA Elsaied H.E., Naganuma T.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAA94450.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11282630; DOI=10.1128/AEM.67.4.1751-1765.2001;
RA Elsaied H., Naganuma T.;
RT "Phylogenetic diversity of ribulose-1,5-bisphosphate carboxylase/oxygenase
RT large-subunit genes from deep-sea microorganisms.";
RL Appl. Environ. Microbiol. 67:1751-1765(2001).
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DR EMBL; AB040526; BAA94450.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LBG7; -.
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 Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR Pfam; PF00016; RuBisCO_large; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 4: Predicted;
FT DOMAIN 1..107
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA94450.1"
FT NON_TER 109
FT /evidence="ECO:0000313|EMBL:BAA94450.1"
SQ SEQUENCE 109 AA; 11708 MW; 8C9AEEEE3CE64209 CRC64;
EPFADACYQF WLGGDFVKND EPQGNQVFAP FRQTITAVAD AMARAQDATG AAKLYSANIT
ADDPFEMIAP RECILDTFGC NAAQVNFLVD GYAGGPAAIT TARRQFPGH
//