ID   D8ICR0_BRAP9            Unreviewed;       754 AA.
AC   D8ICR0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit-like protein {ECO:0000313|EMBL:ADK30933.1};
GN   OrderedLocusNames=BP951000_0935 {ECO:0000313|EMBL:ADK30933.1};
OS   Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30933.1, ECO:0000313|Proteomes:UP000000332};
RN   [1] {ECO:0000313|EMBL:ADK30933.1, ECO:0000313|Proteomes:UP000000332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX   PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA   Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA   Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT   "The complete genome sequence of the pathogenic intestinal spirochete
RT   Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL   PLoS ONE 5:E11455-E11455(2010).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002025; ADK30933.1; -; Genomic_DNA.
DR   RefSeq; WP_013243887.1; NC_014330.1.
DR   AlphaFoldDB; D8ICR0; -.
DR   STRING; 759914.BP951000_0935; -.
DR   GeneID; 56439498; -.
DR   KEGG; bpo:BP951000_0935; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1013; Bacteria.
DR   HOGENOM; CLU_020913_0_0_12; -.
DR   InParanoid; D8ICR0; -.
DR   Proteomes; UP000000332; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; 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; -; 3.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
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   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:ADK30933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000332};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          24..248
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          270..375
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   DOMAIN          538..657
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   754 AA;  82866 MW;  03F5296F6ED12966 CRC64;
     MAQKYNLAEQ ENILESGNEL AAIAAAQINY HVMGYYPITP STQIAEYLDE MKANGRHTVC
     MIPGDGEHGA AGICYGATTA GGRVFNATSA NGLLFAMEQL PVQAGTRFPM VLNVVNRTVS
     GPLDIKCDQS DIMMALNTGW IIIMAHTTQM VYDFNIFALK IAEKAKLPII VSSDGFFTSH
     QKKKIHLFKN DKDVQDFLGK YTPEVTSVEP TKNPVTIGPY MNEDELTGSK LQLSQALEDS
     RAIIAEVFEE FASLSGRKYS PIETHNMEGA EVALMLCGSA YETGTLAVDE MRKANPNLKI
     GAFAITQIRP FPEKELQKLL ANVKVVVVGD RQDTYSGMGG NMSTEIRAAL KNDPNNKSSI
     VSRVYGLGGT EFTLDKAKEL FELGLKELAK AGSVEKHSYL EQYMGDPNVK MKPIHEPLTL
     ESQKSGITVT MNEQTHKLDV KVPPLRELTG KAYRYAQGHG ACNGCGIFSG INTFMKGIEG
     SVVLLVHTGC SMVVTTGYPY SSYRTTYVHN LFQNGAATLS GIVEMYHERK RRGEIDGPED
     PTFIMVTGDG GHDIGMGPSI GAAIRNHKMI ILEYDNEGYM NTGNQLSFST PLGHRTSTSN
     VGKAEVGKQF GHKDVAQIFN GCHIPYIATG CEAYPLDLVK KAAKAQWYAN NVGTAFVKLL
     ITCPLNWKTP DDMGKDIIKA AVDCCFFPLY EVEQGITTIT NMVADDKKQP VTEWLKLMGK
     TKHLLKHQDI LDKFQADVDN RWARLKAMHE SPVL
//