ID   A0A1H0XX56_9FLAO        Unreviewed;       699 AA.
AC   A0A1H0XX56;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:SDQ07482.1};
GN   ORFNames=SAMN05421664_0332 {ECO:0000313|EMBL:SDQ07482.1};
OS   Chryseobacterium soldanellicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=311333 {ECO:0000313|EMBL:SDQ07482.1, ECO:0000313|Proteomes:UP000199627};
RN   [1] {ECO:0000313|EMBL:SDQ07482.1, ECO:0000313|Proteomes:UP000199627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17072 {ECO:0000313|EMBL:SDQ07482.1,
RC   ECO:0000313|Proteomes:UP000199627};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNKL01000001; SDQ07482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0XX56; -.
DR   STRING; 311333.SAMN05421664_0332; -.
DR   Proteomes; UP000199627; 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          363..539
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   699 AA;  78256 MW;  2DDF1D79D6D426FE CRC64;
     MFFYVYLLPM ENTLHEKVSQ DILLKAYNHM MLAKAMADIY EENRNVCKYV HSTSRGHEAI
     QLATAYQLKK EDWVSPYYRD ESILLGIGFE PYQLMLQLLA KADDPFSGGR SYYSHPSSRD
     ENMPKIIHQS SATGMQTIPT TGVAQGIKYI QDFELQNFEN NPVVVCSLGD NSVTEGEVSE
     ALQFAALHQL PIIFLVQDNE WGISVTKEEA RTCDAYDFVA GFVGLGRMRV DGTDFVESFE
     VMKKAVDFVR TERKPLVVCA KTVLIGHHTS GVRREFYRDE EDLTKHRAKD PGEILRKQLL
     ESGADEELLK QITKKARLEA EEAFERAQNA EDPKPETVMQ HIFAPTPITE EVGTREPEGG
     EKIVMVDAAI HAIQEIMWKH PEALLYGQDV GERIGGVFRE TVTLGKKFGS KRVFNTAIQE
     AYIIGSTTGM SAVGLKPIVE VQFADYIYPG INQLITEISK SNYLSNGKFP VSNIIRVPIG
     AYGGGGPYHS GSVESILANI KGIKIAYPSN AADFKGLLKA AYYDPNPVVM LEHKGLYWSK
     VPGTEDAKTI EPAEDYVLPF GKGKIIIEAD KEQTEKGRTL LVVTYGMGVY WAKEAAKSFN
     GRVEVIDLRT LIPLDEELVF ERVKAHGKCI VLTEEQLNNS FAEAFAHRIS KNCFKYLDAP
     VETMGSLDTP AVPINLILEK EMLPNAEKLS IKIEEMLKY
//