ID   Q890V9_CLOTE            Unreviewed;       396 AA.
AC   Q890V9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Pyruvate synthase subunit porA {ECO:0000313|EMBL:AAO36986.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:AAO36986.1};
GN   Name=porA {ECO:0000313|EMBL:AAO36986.1};
GN   OrderedLocusNames=CTC_02526 {ECO:0000313|EMBL:AAO36986.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36986.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO36986.1, ECO:0000313|Proteomes:UP000001412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA   Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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DR   EMBL; AE015927; AAO36986.1; -; Genomic_DNA.
DR   RefSeq; WP_011100647.1; NC_004557.1.
DR   AlphaFoldDB; Q890V9; -.
DR   STRING; 212717.CTC_02526; -.
DR   GeneID; 24254674; -.
DR   KEGG; ctc:CTC_02526; -.
DR   HOGENOM; CLU_002569_5_0_9; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000001412; 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:AAO36986.1};
KW   Pyruvate {ECO:0000313|EMBL:AAO36986.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT   DOMAIN          20..243
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          266..370
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   396 AA;  43422 MW;  345A4A596A49FEF8 CRC64;
     MLKDNQIRKS LSGNEAVAIA MKQIEPDVVA AFPITPFTEV PQYFSTFVAE GKCNTEFVPV
     ESEHSAMSAC VGASSAGARV MTATSSNGLG LMWEMLHIAA GDRCPIILAL VNRAMSPPLN
     IHNDHSDSMG ARDAGWIQIY SENTQEAYDN FIQIVKVAEN EKVMVPAMVC YDGFITSHAV
     ENVTLLEDSA VKEFVGENKR VNDGLLGEDS MAVGPMVLTD FYMEMKRSQL QGLLNAKEVL
     LEVSKEYEKL TGRKYGLFEE YKLSDADIAM VIIGSSAGTG KKVVDDLREK GIKAGLLKIR
     LYRPFPGKEI AKALKNVKAL AVMDKAEGLS GNGGPIFTDV SAAIYGELKD AILMSYIYGL
     GGRDVRVEDL EKVFMELKEA METGNYDKYN YLSLRE
//