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Database: UniProt
Entry: D3HX09_9BACT
LinkDB: D3HX09_9BACT
Original site: D3HX09_9BACT 
ID   D3HX09_9BACT            Unreviewed;       360 AA.
AC   D3HX09;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=3-methyl-2-oxobutanoate dehydrogenase (Ferredoxin) {ECO:0000313|EMBL:EFC76169.1};
DE            EC=1.2.7.7 {ECO:0000313|EMBL:EFC76169.1};
GN   ORFNames=HMPREF0649_00791 {ECO:0000313|EMBL:EFC76169.1};
OS   Segatella buccae D17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=575611 {ECO:0000313|EMBL:EFC76169.1, ECO:0000313|Proteomes:UP000005080};
RN   [1] {ECO:0000313|EMBL:EFC76169.1, ECO:0000313|Proteomes:UP000005080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D17 {ECO:0000313|EMBL:EFC76169.1,
RC   ECO:0000313|Proteomes:UP000005080};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Sibley C.D., White A., Allen-Vercoe E., Strauss J., Crowley S.,
RA   Surette M.G., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG739929; EFC76169.1; -; Genomic_DNA.
DR   RefSeq; WP_004341297.1; NZ_GG739929.1.
DR   AlphaFoldDB; D3HX09; -.
DR   HOGENOM; CLU_017038_0_0_10; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000005080; Unassembled WGS sequence.
DR   GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) 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; PTHR43088; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43088:SF1; SUBUNIT OF 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:EFC76169.1}.
FT   DOMAIN          17..232
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          257..351
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   360 AA;  39278 MW;  4DF279D727EE5A45 CRC64;
     MAEQEITLMK GNEAIAHAAI RCGADGYFGY PITPQSEIIE TLALLKPWET TGMVVLQAES
     EVASINMVYG GAGAGKRVMT TSSSPGIALM QEGISYMAGA ELPGVFVNVQ RGGPGLGTIQ
     PSQSDYFQAT RGGGNGDYNV IVLAPASVQE MADFVDLAFE LAFKYRNPAM ILSDGVIGQM
     MEKVVLPPMK PRRTEEQIKK ECPWASIGRT RDREPNIITS LELKPEVMEM RNLHLQEKYR
     RIKETEVRYE TTLCDDADYL IVAFGSASRI AEKSVETARA KGIKVGLFRP ITLWPFPSKE
     IMEASKGKKG ILVAEINAGQ MVEDVRLAVN GTIPVDHFGR LGGIVPDPEE IVKALKSLPE
//
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