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
//