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Database: UniProt
Entry: A0A0Q3TTB9_9BACI
LinkDB: A0A0Q3TTB9_9BACI
Original site: A0A0Q3TTB9_9BACI 
ID   A0A0Q3TTB9_9BACI        Unreviewed;       288 AA.
AC   A0A0Q3TTB9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:KQL35580.1};
GN   ORFNames=AN959_06680 {ECO:0000313|EMBL:KQL35580.1};
OS   Psychrobacillus sp. FJAT-21963.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL35580.1, ECO:0000313|Proteomes:UP000051878};
RN   [1] {ECO:0000313|EMBL:KQL35580.1, ECO:0000313|Proteomes:UP000051878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL35580.1,
RC   ECO:0000313|Proteomes:UP000051878};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) 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:KQL35580.1}.
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DR   EMBL; LJIY01000002; KQL35580.1; -; Genomic_DNA.
DR   RefSeq; WP_053589911.1; NZ_LJIY01000002.1.
DR   AlphaFoldDB; A0A0Q3TTB9; -.
DR   PATRIC; fig|1712028.3.peg.2601; -.
DR   Proteomes; UP000051878; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000051878}.
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;  31274 MW;  BE6F1D6D1A2F25BE CRC64;
     MVTFKDFRNN VKPNWCPGCG DFSVQAAIQR AAANVGIQPH DLAVISGIGC SGRISGYIHS
     YGFHGIHGRA LPIAQGLKMA NKDLHVIASG GDGDGFAIGI GHTIHSIRRN IDLTYVVMDN
     QIYGLTKGQT SPRSAEGFKT KSTPGGAIEP SLKPLELALT SGATFVAQGF SSDIKELTAI
     IEAGINHKGF SFINVFSPCV TYNKVNTYDW FKEHLTKLSN VEGYDHTSRE DALKVVMETE
     GLVTGIIYQN ENAPSYQEQA PGYAQTPLVD QNLKMSEQEF NALLQDFM
//
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