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Database: UniProt
Entry: A0A0G1L1D0_9BACT
LinkDB: A0A0G1L1D0_9BACT
Original site: A0A0G1L1D0_9BACT 
ID   A0A0G1L1D0_9BACT        Unreviewed;       295 AA.
AC   A0A0G1L1D0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=2-oxoacid ferredoxin oxidoreductase beta subunit {ECO:0000313|EMBL:KKT53939.1};
GN   ORFNames=UW45_C0022G0009 {ECO:0000313|EMBL:KKT53939.1};
OS   Parcubacteria group bacterium GW2011_GWC2_44_22.
OC   Bacteria.
OX   NCBI_TaxID=1618930 {ECO:0000313|EMBL:KKT53939.1, ECO:0000313|Proteomes:UP000034136};
RN   [1] {ECO:0000313|EMBL:KKT53939.1, ECO:0000313|Proteomes:UP000034136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KKT53939.1}.
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DR   EMBL; LCII01000022; KKT53939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1L1D0; -.
DR   PATRIC; fig|1618930.3.peg.783; -.
DR   Proteomes; UP000034136; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR011896; OFOB.
DR   InterPro; IPR032686; PFO_beta_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR02177; PorB_KorB; 1.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF12367; PFO_beta_C; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          57..204
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          208..272
FT                   /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12367"
SQ   SEQUENCE   295 AA;  32577 MW;  2E776B2B95A31142 CRC64;
     MLSDNQQPTP LTIADYANTM FPTWCPGCGN HGLLVAMKQA LAELQLQPHK LFFVWGIGCS
     SNTSNWVNVY GAHSLHGRAL PVAVAIKLVN PALTVIAEGG DGDGYGIGVG HFIHSMRRNL
     DITYIVHNNQ IYGLTTGQAS PTSDKGMKSK STPCGVIERP INPLALAISS NATYIARGFS
     GDVAHLKQLI MGGIKHRGFA LIDVLQPCVT FNNQNTYPWV QERVYKLEGT GHDPKDKAQA
     WQRAQEWGDK IPIGLFFQED RLTYRDEIDQ FAKDESLLDH DISNIDISKT LEEFK
//
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