ID   A0LSR4_ACIC1            Unreviewed;       396 AA.
AC   A0LSR4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   02-APR-2025, entry version 84.
DE   SubName: Full=Pyruvate ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:ABK52474.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:ABK52474.1};
GN   OrderedLocusNames=Acel_0701 {ECO:0000313|EMBL:ABK52474.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales;
OC   Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52474.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52474.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032}.
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DR   EMBL; CP000481; ABK52474.1; -; Genomic_DNA.
DR   RefSeq; WP_011719537.1; NC_008578.1.
DR   AlphaFoldDB; A0LSR4; -.
DR   STRING; 351607.Acel_0701; -.
DR   KEGG; ace:Acel_0701; -.
DR   eggNOG; COG0674; Bacteria.
DR   HOGENOM; CLU_002569_5_0_11; -.
DR   InParanoid; A0LSR4; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:TreeGrafter.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   FunFam; 3.40.50.970:FF:000012; Pyruvate:ferredoxin (Flavodoxin) oxidoreductase; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR050722; Pyruvate:ferred/Flavod_OxRd.
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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABK52474.1}; Pyruvate {ECO:0000313|EMBL:ABK52474.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT   DOMAIN          15..231
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          258..352
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   396 AA;  42445 MW;  EA3059D891C1B9BF CRC64;
     MRSQREASRA IAEVVGRCRP QVVPAYPITP QTHIVEALGA MIRAGTLSPC VFLTVESEFA
     AMSAAIGASF AGSRTYTATA SQGLLYMAEA LFNASGLGAP IVMTVANRAV GAPINIWNDQ
     SDAMSLRDCG WIQLYAPDNQ AAVDLHVLAF RVAEALSLPV MVCMDGFVLT HAFEPLAVPT
     QAQVDNFLPP FRPRQVLDPG DPVTIGAMVG PEAFTEVKYL SAQRLDAAVN VFEWFAQEYA
     EITGRRYHAV ESYRIEHADT VVVALGSAAG TLYELADAVP GVGVLVITMY RPFPARVVRG
     LLAAARRVIV LERAFAPGAG GIVTADVRAA VAGTSAMVHT VIGGLGGRPI RLASLRAVVT
     ADALPDIHFL DLREDVVRRE WERDPTVSAM EVRHVR
//