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Database: UniProt
Entry: A0A101GJR3_9BACT
LinkDB: A0A101GJR3_9BACT
Original site: A0A101GJR3_9BACT 
ID   A0A101GJR3_9BACT        Unreviewed;       378 AA.
AC   A0A101GJR3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   28-JUN-2023, entry version 31.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:KUK59475.1};
GN   ORFNames=XD80_0004 {ECO:0000313|EMBL:KUK59475.1};
OS   Synergistales bacterium 53_16.
OC   Bacteria; Synergistota; Synergistia; Synergistales.
OX   NCBI_TaxID=1635273 {ECO:0000313|EMBL:KUK59475.1, ECO:0000313|Proteomes:UP000053116};
RN   [1] {ECO:0000313|Proteomes:UP000053116}
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:KUK59475.1}.
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DR   EMBL; LGGB01000001; KUK59475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101GJR3; -.
DR   PATRIC; fig|1635273.3.peg.544; -.
DR   Proteomes; UP000053116; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:KUK59475.1}.
FT   DOMAIN          16..251
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          276..370
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   378 AA;  42111 MW;  FD423CBE0CF46A73 CRC64;
     MKNETNFWQG NVALAHGALA AGCRFFGGYP ITPSSEIAEV MAEELPKLNG RFIQMEDEIA
     GIAAAIGASM TGKKSMTATS GPGFSLKQEN LGLAYMAEIP LVVVDVMRGG PSTGLPTSIS
     QQDVMQARWG THGDHATIAY APSSVQECYE TAIKAFNMAE RFRQPVLIMS DEVLGHMRER
     VTIQKDMMPK IINRKRPAVD PDEFKPYKPD DEDNLPPMAS FGDGYRWHIT GLTHNEWGFP
     TNDPEEIEKK TRRLMDKVSA YRDEIVEYET ESVNDAEILV VSYGSVARTA LSAVRMARKK
     GLKAGSFRLV TLWPFPDREI ENIAERSRVI LVPELNYGQM VLETERAVHG KARVVPYNLV
     NGELFKPEEI LEKIEEVG
//
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