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Database: UniProt
Entry: A0A101I5R1_9BACT
LinkDB: A0A101I5R1_9BACT
Original site: A0A101I5R1_9BACT 
ID   A0A101I5R1_9BACT        Unreviewed;       388 AA.
AC   A0A101I5R1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:KUK88969.1};
GN   ORFNames=XE01_0152 {ECO:0000313|EMBL:KUK88969.1};
OS   Synergistales bacterium 58_81.
OC   Bacteria; Synergistota; Synergistia; Synergistales.
OX   NCBI_TaxID=1635274 {ECO:0000313|EMBL:KUK88969.1, ECO:0000313|Proteomes:UP000054873};
RN   [1] {ECO:0000313|Proteomes:UP000054873}
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:KUK88969.1}.
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DR   EMBL; LGGV01000003; KUK88969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101I5R1; -.
DR   STRING; 1635274.XE01_0152; -.
DR   PATRIC; fig|1635274.3.peg.126; -.
DR   Proteomes; UP000054873; 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; 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   Pyruvate {ECO:0000313|EMBL:KUK88969.1}.
FT   DOMAIN          15..239
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          262..363
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   388 AA;  42747 MW;  01FF1646F9D9DAE3 CRC64;
     MSRKDITSGN WAVAEAMRQI NPDVVAAYPI TPSTDIPMKF SEFVADGLVD TNLVTVESEH
     SAISACLAAA VSGARVMTAS SANGVALMHE IFPIAASYRA PIVFGLVNRS LGAPINIHCD
     HSDSMAERDS GWIHIYCEDG QEVYDTMIMA VRIAEHKDVL LPVFVCQDGF ITSHCFEPVE
     FMDDEEVRSF IGERDPLFPL LDIDNPVAYG SLALTDYYFE IKRQQVEAMK HVERVYREVA
     GEFAKKTGRD YPVVDTYKTD DADHIMVIMS SAAGAAKDTV DRLREKGHKV GCLRIRLFRP
     FPAKAVVDAL KGAKSIAVLD RAASLGAPAP LFTEIKGALY DAGIHIPANT YVYGLGGRDF
     FPHNAEEAFM DLINNNMSPE ERYLGLRE
//
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