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Database: UniProt
Entry: A0A0S8KNN3_9CHLR
LinkDB: A0A0S8KNN3_9CHLR
Original site: A0A0S8KNN3_9CHLR 
ID   A0A0S8KNN3_9CHLR        Unreviewed;       397 AA.
AC   A0A0S8KNN3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KPL23354.1};
GN   Name=porA {ECO:0000313|EMBL:KPL23354.1};
GN   ORFNames=AMJ93_04925 {ECO:0000313|EMBL:KPL23354.1};
OS   Anaerolineae bacterium SM23_84.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL23354.1, ECO:0000313|Proteomes:UP000052016};
RN   [1] {ECO:0000313|EMBL:KPL23354.1, ECO:0000313|Proteomes:UP000052016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_84 {ECO:0000313|EMBL:KPL23354.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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:KPL23354.1}.
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DR   EMBL; LJUZ01000051; KPL23354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8KNN3; -.
DR   PATRIC; fig|1703388.3.peg.161; -.
DR   Proteomes; UP000052016; 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:KPL23354.1}.
FT   DOMAIN          18..241
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          264..369
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   397 AA;  42799 MW;  4902F7A3F41A2D97 CRC64;
     MVKSTRLALD GAHAASTAMR QINPDVVAAY PITPQTAVVQ TFSQYVADGV VDTEFMAVES
     EHAAMSACIG ASAAGGRVMT ATAANGLALM WEMVYIAASM RLPIVMTVVN RALSAPLNIH
     CDHSDSMGAR DAGWIQLYSE TAQEAYDNLI QAVRIAEHPD LLLPVMVMQD GFITGHGVER
     VEVLDEGLVK EFIGTYKPKY SLLDVDEPKT FGAWDMYDYY FEHKRQQTDA FSKAMNVIVD
     VGEEYGQLSG RGYGIFESYA LDDAEMAIVV LSSASGTARS VVKKLRGEGV KIGLLKPRVF
     RPFPSQELAA ALKGVKAVAV LDRSISFGAM DGAGPLYLEL CAALFASGLG TKVVNYIFGL
     GGRDIFPEHF EQVASDLQQI AATGEVKSLV GYLGLRE
//
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