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Database: UniProt
Entry: A0A1B6B9S8_9FIRM
LinkDB: A0A1B6B9S8_9FIRM
Original site: A0A1B6B9S8_9FIRM 
ID   A0A1B6B9S8_9FIRM        Unreviewed;       393 AA.
AC   A0A1B6B9S8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Pyruvate:ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:GAU76463.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:GAU76463.1};
GN   ORFNames=F3D3_1060 {ECO:0000313|EMBL:GAU76463.1};
OS   Fusibacter sp. 3D3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX   NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU76463.1, ECO:0000313|Proteomes:UP000095197};
RN   [1] {ECO:0000313|EMBL:GAU76463.1, ECO:0000313|Proteomes:UP000095197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D3 {ECO:0000313|EMBL:GAU76463.1,
RC   ECO:0000313|Proteomes:UP000095197};
RA   Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA   Demergasso C.S.;
RT   "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT   arsenic level Ascotan salt flat in northern Chile.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:GAU76463.1}.
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DR   EMBL; BDHH01000003; GAU76463.1; -; Genomic_DNA.
DR   RefSeq; WP_069871797.1; NZ_BDHH01000003.1.
DR   AlphaFoldDB; A0A1B6B9S8; -.
DR   STRING; 1048380.F3D3_1060; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000095197; Unassembled WGS sequence.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:GAU76463.1};
KW   Pyruvate {ECO:0000313|EMBL:GAU76463.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095197}.
FT   DOMAIN          16..239
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          262..366
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   393 AA;  43153 MW;  F425383CADFBACC8 CRC64;
     MTIRDRLSGN EAVAIAMKQI NPDVMPAFPI TPSTEIPQYF SQYVANGEVD TVFIPVESEH
     SAMSACIGSE GAGARTFTAT SSCGLALMHE MLYVASSSRL PITLACVNRA LTGPININND
     HSDSMGSRDA GWIQIYSENN QEAYDNFIQA VKIAEHKDIM LPAMVCQDGF ITSHAVENIE
     LIEDAKVKAF VGEYEPEDFL LNPNSPIAIG PYDTASFYIE HKRQQAEAMI KVKEIALEVA
     AEFEKISGRK YGLFETYELE DADTALVIIN STAGTAKDAI DKLRAEGKKV GLLKIRLFRP
     FPREEIAEAL KHIKAIAVMD KCEGFSAAGG PLFAEVRSAL YDLNEKPMTV NYIYGLGGRD
     VRTTDIESVY SDLDTIVESG KAGDTYRYLG VRE
//
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