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Database: UniProt
Entry: A3J7C8_9FLAO
LinkDB: A3J7C8_9FLAO
Original site: A3J7C8_9FLAO 
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
//
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