ID E0WH95_9ZZZZ Unreviewed; 119 AA.
AC E0WH95;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase form I large subunit {ECO:0000313|EMBL:CBN08517.1};
DE Flags: Fragment;
GN Name=cbbL {ECO:0000313|EMBL:CBN08517.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:CBN08517.1};
RN [1] {ECO:0000313|EMBL:CBN08517.1}
RP NUCLEOTIDE SEQUENCE.
RA Perner M., Petersen J.M., Zielinski F., Gennerich H.H., Seifert R.;
RT "Geochemical constraints on the diversity and activity of H2-oxidizing
RT microorganisms in diffuse hydrothermal fluids from a basalt- and an
RT ultramafic-hosted vent.";
RL FEMS Microbiol. Ecol. 74:55-71(2010).
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DR EMBL; FN908931; CBN08517.1; -; Genomic_DNA.
DR AlphaFoldDB; E0WH95; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_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 SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
PE 4: Predicted;
FT DOMAIN 1..119
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:CBN08517.1"
FT NON_TER 119
FT /evidence="ECO:0000313|EMBL:CBN08517.1"
SQ SEQUENCE 119 AA; 13198 MW; F8120B1D25D133C3 CRC64;
FVMQAIHKAE ADTGERKGHY LNVTAATADE MMKRAEYAKE IGAPIIMHDY ITGGWSANTQ
LAQWCQENGL LLHIHRAMHA VLDRNPHHGI HFRVLAKILR LSGGDHLHSG TVVGKLEGD
//