ID C6JJQ0_FUSVA Unreviewed; 354 AA.
AC C6JJQ0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=3-methyl-2-oxobutanoate dehydrogenase (Ferredoxin) {ECO:0000313|EMBL:EES64963.1};
DE EC=1.2.7.7 {ECO:0000313|EMBL:EES64963.1};
GN ORFNames=FVAG_01646 {ECO:0000313|EMBL:EES64963.1};
OS Fusobacterium varium ATCC 27725.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469618 {ECO:0000313|EMBL:EES64963.1, ECO:0000313|Proteomes:UP000004505};
RN [1] {ECO:0000313|EMBL:EES64963.1, ECO:0000313|Proteomes:UP000004505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES64963.1,
RC ECO:0000313|Proteomes:UP000004505};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium varium ATCC 27725.";
RL Submitted (MAY-2011) 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:EES64963.1}.
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DR EMBL; ACIE02000015; EES64963.1; -; Genomic_DNA.
DR RefSeq; WP_005949604.1; NZ_GL987996.1.
DR AlphaFoldDB; C6JJQ0; -.
DR STRING; 469618.FVAG_01646; -.
DR GeneID; 77466705; -.
DR eggNOG; COG0674; Bacteria.
DR HOGENOM; CLU_017038_0_0_0; -.
DR Proteomes; UP000004505; 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:EES64963.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004505}.
FT DOMAIN 15..241
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 248..342
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 354 AA; 38974 MW; C989424B66BA619C CRC64;
MKKKLMKGSE VLGASAIKAG CLHFFGYPIT PQNEIPEYMS KELPKIEGGT FVQAESEVAA
INMVYGSAST GVRCMTSSSS PGIALKQEGI AYCCGAELPC VIGSVSRGGP GLGSIQPAQS
DYFQATRGGG NGDYRVIVYA PYNLQELSDL TQKAFYMADK YRNPVMLLLD GTIAQMMEGV
EIRDITFPPI DKSNWAITGK KGRKEHHIIT SIYLDTDTCE KHNHKLFKKY DEIEKNEAEV
ELYLTDDAEI IIASYGTSAR IVKNAINDLR KKGIKAGLIR PITLWPFPYA AFKNISEPCK
AVMSIELSMG QMIQDVKIGV AGKYEIGFYG RCGGNLFDSE EVVNAIEKYY KEVK
//
