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Database: UniProt
Entry: A0A1M6QUU3_9FLAO
LinkDB: A0A1M6QUU3_9FLAO
Original site: A0A1M6QUU3_9FLAO 
ID   A0A1M6QUU3_9FLAO        Unreviewed;       658 AA.
AC   A0A1M6QUU3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:SHK24004.1};
GN   ORFNames=SAMN04488007_2492 {ECO:0000313|EMBL:SHK24004.1};
OS   Maribacter aquivivus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=228958 {ECO:0000313|EMBL:SHK24004.1, ECO:0000313|Proteomes:UP000184314};
RN   [1] {ECO:0000313|EMBL:SHK24004.1, ECO:0000313|Proteomes:UP000184314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16478 {ECO:0000313|EMBL:SHK24004.1,
RC   ECO:0000313|Proteomes:UP000184314};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FQZX01000002; SHK24004.1; -; Genomic_DNA.
DR   RefSeq; WP_073244603.1; NZ_FQZX01000002.1.
DR   AlphaFoldDB; A0A1M6QUU3; -.
DR   STRING; 228958.SAMN04488007_2492; -.
DR   Proteomes; UP000184314; 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}.
FT   DOMAIN          341..514
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   658 AA;  73964 MW;  8D947509CB0D7D4D CRC64;
     MNYTDFKVAK DVKLKLYKSM LKPRMIEEKM LILLRQGKIS KWFSGIGQEA ISIGVTTALN
     SDEYILPMHR NLGVFTTRDI PLYRLFTQWQ GKASGFTQGR DRSFHFGTQE FKIVGMISHL
     GPQLGVADGI ALAHKLKKEK KVTAVFTGEG ATSEGDFHEA LNVASVWSLP VLFCVENNGY
     GLSTPTNEQF KCENIADKGV GYGMESHIID GNNILEVYFK VADLIRDMRI NPRPVLLEFK
     TFRMRGHEEA SGTKYVPQEL LDTWAEKDPL ENFTQYLLRE NILTEESIAN FKAEIQSEID
     EHLKIAFAEE AIIPNQSKEL SEVYKKFDLK EVEPSKFVTN IRLVDAISEG LRQSMKKFDN
     LVIMGQDVAE YGGVFKITDG FVNDFGKERV RNTPICESAI VSAAMGLSIN GMKAVMEMQF
     ADFASSGFNP IVNYLAKSFY RWGENADVVI RMPCGGGVSA GPFHSQTNEA WFTKTPGLKV
     VYPAFPYDAK GLLATSIEDP NPVLFFEHKG LYRSFYQEVP VDYYTLPLGK ASLLKQGDQI
     TIVTYGAGVH WALETLEKNT DIRADLLDLR TLQPLDINAI YDSVKRTGKL IILQEDSLFG
     GIASDISAMV MENCFEYLDG PIKRVGSLET PIPFNTKLEE QYLAKSRFES DLKELIAY
//
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