ID A3J7C8_9FLAO Unreviewed; 658 AA.
AC A3J7C8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion {ECO:0000313|EMBL:EAZ94451.1};
GN ORFNames=FBBAL38_12175 {ECO:0000313|EMBL:EAZ94451.1};
OS Flavobacteria bacterium BAL38.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391598 {ECO:0000313|EMBL:EAZ94451.1, ECO:0000313|Proteomes:UP000003784};
RN [1] {ECO:0000313|EMBL:EAZ94451.1, ECO:0000313|Proteomes:UP000003784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL38 {ECO:0000313|EMBL:EAZ94451.1,
RC ECO:0000313|Proteomes:UP000003784};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EAZ94451.1}.
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DR EMBL; AAXX01000008; EAZ94451.1; -; Genomic_DNA.
DR AlphaFoldDB; A3J7C8; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000003784; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003784}.
FT DOMAIN 341..514
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 658 AA; 73963 MW; 658033C2BB8594E1 CRC64;
MNFERKELTN PQLLDLYKKI LKPRLIEEKM LILIRQGKVS KWFSGIGQEA ISVGITSVLD
KDEYILPMHR NLGVFTTRDI PLHRLFSQWQ GKKNGFTKGR DRSFHFGTQE YKIIGMISHL
GPQLGIADGI ALANKLRKNG KVTAVFTGEG ATSEGDFHEA LNIAAVWELP VLFVIENNGY
GLSTPTNEQY RCENLADKGV GYGMESHVVD GNNLLEVVHL ISELKASMVE NPRPVLLEFK
TFRMRGHEEA SGTKYVPQEL MDMWAIKDPV ENYRNYLKVT AVLSDEEDEA IRAEIKKEID
TDWAKVQEEP AIVASLEEEL GDVYAPYDFE AFNPSLEVEN IRVIDAISNG LRQSMERHEN
LVIMGQDIAE YGGAFKITDG FVAQFGKERV RNTPICESAV VSAANGLSIN GFKAVMEMQF
ADFVSTGFNP IVNLLAKQHY RWNEKSDVVV RMPCGGGTQA GPFHSQTNEA WFTKTPGLKV
VYPAFPYDAK GLLNTAINDP NPVLFFEHKQ LYRSVYQDVP KDYYTLPFGK ASLIKEGTDV
TIISFGAGVH WALETLAKNP EIKADLLDLR TLQPMDWDAI YASVKKTNKV IILQEDTLFG
GVASDISAMI MENCFEQLDA PVRRVGSLES AIPFMKSLED QYLPKVRFET ELKELLAY
//