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Database: UniProt
Entry: A0A0F2PX28_9FIRM
LinkDB: A0A0F2PX28_9FIRM
Original site: A0A0F2PX28_9FIRM 
ID   A0A0F2PX28_9FIRM        Unreviewed;       361 AA.
AC   A0A0F2PX28;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Ferredoxin oxidoreductase {ECO:0000313|EMBL:KJS18005.1};
GN   ORFNames=VR69_02520 {ECO:0000313|EMBL:KJS18005.1};
OS   Peptococcaceae bacterium BRH_c4b.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS18005.1, ECO:0000313|Proteomes:UP000033446};
RN   [1] {ECO:0000313|EMBL:KJS18005.1, ECO:0000313|Proteomes:UP000033446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS18005.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS18005.1}.
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DR   EMBL; LADO01000009; KJS18005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2PX28; -.
DR   STRING; 1629717.VR69_02520; -.
DR   PATRIC; fig|1629717.3.peg.231; -.
DR   Proteomes; UP000033446; 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;
FT   DOMAIN          23..251
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          261..334
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   361 AA;  39890 MW;  8F346295C97FB117 CRC64;
     MSDKPIQGEK RVFMTGNEVV AYAALAARAE IMYGYPITPQ NEIMHYWTRM APKYNREFLQ
     TEDELSAGFT TLGGVLAGKK AFTATAGPGN TLMQEPLSMA EAMRLPSVVV VQQRGGPSTA
     TVIYSQQEVT LTTLGGNGEG LRVVYSTSTH QELFDYTIKA FNTAWKYKFP TFVLGDGYQA
     KMRESLTMYD PGEKGIELIP AEAYLGKPGT PGVDRPPAHY RNTYNVEEEL YEVLQGHFKD
     YEKMAPEVTE YESFGVEDST LVVVSHGVVA RAAKEAVREL REAGVKVGYF RPITLRPLPE
     KQLREAAARA GRFLVMESAQ GQLGRLLKEA IFGAPVEMIP FYKPGVGITS EEVVDKVKAT
     I
//
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