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Database: UniProt
Entry: A0A124FP98_9FIRM
LinkDB: A0A124FP98_9FIRM
Original site: A0A124FP98_9FIRM 
ID   A0A124FP98_9FIRM        Unreviewed;       356 AA.
AC   A0A124FP98;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Pyruvate:ferredoxin oxidoreductase alpha subunit {ECO:0000313|EMBL:KUK52166.1};
GN   ORFNames=XD78_2174 {ECO:0000313|EMBL:KUK52166.1};
OS   Desulfotomaculum sp. 46_296.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK52166.1, ECO:0000313|Proteomes:UP000053813};
RN   [1] {ECO:0000313|Proteomes:UP000053813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK52166.1}.
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DR   EMBL; LGFZ01000103; KUK52166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124FP98; -.
DR   STRING; 1635262.XD78_2174; -.
DR   PATRIC; fig|1635262.3.peg.1434; -.
DR   Proteomes; UP000053813; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; PTHR43088; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43088:SF1; SUBUNIT OF 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   Pyruvate {ECO:0000313|EMBL:KUK52166.1}.
FT   DOMAIN          14..187
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          247..341
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   356 AA;  39083 MW;  9D96FC31F91E1679 CRC64;
     MRRFLMKGND AIGEGAILAG CRHFFGYPIT PQSEVAHYLA KRLPEVGGLF MQAESELASI
     NLVFGAACAG ARVMTASSSP GVSLMQEGLS FLAGSELPCV LVNIMRGGPG LGNIGPSQGD
     YFQATRGGGH GDYYTIVLAP NSVQEILDIM KKAFDLSDMY RMPVVVMADG IMGQMMEPVV
     IDEEKSVEIP PRPWATIGRD YHEDRNEINS LFVVLEEMEE VNLRLLHKYE EIRAKETLCE
     EYMLNDAEVA LVAFGTVSRI CRAVVDKARE QGIRAGLIRP ITLWPFPYDV ISRAAKSAQC
     LLAVEMNMGQ MFEDVEIGAK GRVPVYHYGR LGGMVPLAKD ILEELKKVSE RGGTGR
//
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