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Database: UniProt/TrEMBL
Entry: C0QUF3_PERMH
LinkDB: C0QUF3_PERMH
Original site: C0QUF3_PERMH 
ID   C0QUF3_PERMH            Unreviewed;       397 AA.
AC   C0QUF3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Pyruvate synthase subunit PorA (Pyruvate oxidoreductasealpha chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit alpha) {ECO:0000313|EMBL:ACO03230.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:ACO03230.1};
GN   OrderedLocusNames=PERMA_0529 {ECO:0000313|EMBL:ACO03230.1};
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Persephonella.
OX   NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03230.1, ECO:0000313|Proteomes:UP000001366};
RN   [1] {ECO:0000313|EMBL:ACO03230.1, ECO:0000313|Proteomes:UP000001366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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DR   EMBL; CP001230; ACO03230.1; -; Genomic_DNA.
DR   RefSeq; WP_012675469.1; NC_012440.1.
DR   AlphaFoldDB; C0QUF3; -.
DR   STRING; 123214.PERMA_0529; -.
DR   PaxDb; 123214-PERMA_0529; -.
DR   KEGG; pmx:PERMA_0529; -.
DR   eggNOG; COG0674; Bacteria.
DR   HOGENOM; CLU_002569_5_0_0; -.
DR   OMA; WNDQQDS; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000001366; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
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   Oxidoreductase {ECO:0000313|EMBL:ACO03230.1};
KW   Pyruvate {ECO:0000313|EMBL:ACO03230.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001366}.
FT   DOMAIN          17..243
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          265..368
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   397 AA;  43970 MW;  328FD30E83967DA6 CRC64;
     MAQTKVVALT GNQAAAEAMR QINFDIAAVY PISPQTELMG FFAEYVANGE VDTEMIAVDG
     EHSAMATCIG AAAAGARTIT ASAGPGIAYM VENLYVASGM RVPIVLLDVN RALSAPLSIH
     CDHADSMLTR DTGWISIFCE NAQEAYHSII MSVKISEKAM FPIIVNYDGY IVSHSIEDVE
     ILDDETVRNF VGPSDIHRIP HPLLDIKNPV TYGATAQPDY YTECKYQQHV DFLKVYDVVR
     EVFEEFGQIV GRKYDFIEEY KTEDAEYIGI SMGSSFGTLK DTVDTLREQG KKVGAIKIRL
     YRPFPVKEIA KALSNAKGVA VLDRADSFDG IGGPLFKDVA SALLGTTNRP FVHNFIYGLG
     GREVLEEDFI KAFNRLERLE KGIETRENFV EYLQVRE
//
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