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Database: UniProt
Entry: B0PHK3_9FIRM
LinkDB: B0PHK3_9FIRM
Original site: B0PHK3_9FIRM 
ID   B0PHK3_9FIRM            Unreviewed;       401 AA.
AC   B0PHK3;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain protein {ECO:0000313|EMBL:EDS08971.1};
GN   ORFNames=ANACOL_04296 {ECO:0000313|EMBL:EDS08971.1};
OS   Anaerotruncus colihominis DSM 17241.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS08971.1, ECO:0000313|Proteomes:UP000003803};
RN   [1] {ECO:0000313|EMBL:EDS08971.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS08971.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS08971.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS08971.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2007) 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:EDS08971.1}.
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DR   EMBL; ABGD02000034; EDS08971.1; -; Genomic_DNA.
DR   RefSeq; WP_006877129.1; NZ_DS544193.1.
DR   AlphaFoldDB; B0PHK3; -.
DR   STRING; 169435.ERS852551_01302; -.
DR   eggNOG; COG0674; Bacteria.
DR   HOGENOM; CLU_002569_5_0_9; -.
DR   Proteomes; UP000003803; 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:EDS08971.1}.
FT   DOMAIN          16..240
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          262..363
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   401 AA;  44281 MW;  BA76E610F4002728 CRC64;
     MAHDKMLDGN TAAVEAIKAA RVKVISAYPI TPQSTIAEKL ADAVADGELD ANYVRVESEH
     SALSVALGAQ MTGVRAATAT ASVGLALMHE IVNAAAGVRA PIVMPVVNRA LASPWSLWCD
     HQDSMAERDS GWMQLYCENV QDVYDLTMCA YRIAEDRRVQ LPCMVCLDGF FLSHSMQKVR
     VAEQAEADAF IGPYRRHNSY IDPEDPMIVN NLTSSDEFTE MRYQQSRGFA AAAEVMEEVF
     TEFQERFGRE HHVVEPYRLE DAKTVLVTIG SMAGTAKYVA DRLREQGQHV GVLKIVSFRP
     FPYRQVAALL KNAEHAAVLD RSAGLGAQGA PVWLEVCAAL QSMGINVRGY IGGLGGRDIS
     MDTIRHIFED MAQKDAQVCE EPAWIDLKEH PMNIRQVLKH V
//
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