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Database: UniProt
Entry: A0A150MYF1_9BACI
LinkDB: A0A150MYF1_9BACI
Original site: A0A150MYF1_9BACI 
ID   A0A150MYF1_9BACI        Unreviewed;       288 AA.
AC   A0A150MYF1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=2-oxoglutarate oxidoreductase, beta subunit {ECO:0000313|EMBL:KYD29507.1};
DE            EC=1.2.7.3 {ECO:0000313|EMBL:KYD29507.1};
GN   ORFNames=B4110_1077 {ECO:0000313|EMBL:KYD29507.1};
OS   Parageobacillus toebii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD29507.1, ECO:0000313|Proteomes:UP000075324};
RN   [1] {ECO:0000313|EMBL:KYD29507.1, ECO:0000313|Proteomes:UP000075324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4110 {ECO:0000313|EMBL:KYD29507.1,
RC   ECO:0000313|Proteomes:UP000075324};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KYD29507.1}.
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DR   EMBL; LQYW01000062; KYD29507.1; -; Genomic_DNA.
DR   RefSeq; WP_062678183.1; NZ_LQYW01000062.1.
DR   AlphaFoldDB; A0A150MYF1; -.
DR   PATRIC; fig|153151.4.peg.3465; -.
DR   Proteomes; UP000075324; Unassembled WGS sequence.
DR   GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
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,
KW   ECO:0000313|EMBL:KYD29507.1}.
FT   DOMAIN          49..195
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          199..264
FT                   /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12367"
SQ   SEQUENCE   288 AA;  31490 MW;  483FEB146635B48B CRC64;
     MATFKDFRND VKPNWCPGCG DFSVQAAIQR AAANVGLEPH QLAVISGIGC SGRISGYIHS
     YGFHGTHGRA LPLAQGVKMA NRNLTVIAAG GDGDGFAIGM GHTIHAIRRN IDITYIVMDN
     QIYGLTKGQT SPRSDVGFKT KSTPQGSVEP ALSIMEIALS VGATFVAQSF SSDLKELTSL
     IEEGIKHKGF SLINVFSPCV TYNKVNTYDW FKENLVKVSE IEGYDPSDRA MAMQTVMKYK
     GLVTGLIYQN KEQKSYQELL HGYSETPLAE ADLQLSKEKF DELVSEFM
//
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