ID   A0A1M5FAW4_9BACT        Unreviewed;       662 AA.
AC   A0A1M5FAW4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:SHF88579.1};
GN   ORFNames=SAMN05444008_113115 {ECO:0000313|EMBL:SHF88579.1};
OS   Cnuella takakiae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Cnuella.
OX   NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHF88579.1, ECO:0000313|Proteomes:UP000184368};
RN   [1] {ECO:0000313|EMBL:SHF88579.1, ECO:0000313|Proteomes:UP000184368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26897 {ECO:0000313|EMBL:SHF88579.1,
RC   ECO:0000313|Proteomes:UP000184368};
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; FQUO01000013; SHF88579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5FAW4; -.
DR   STRING; 1302690.BUE76_03330; -.
DR   Proteomes; UP000184368; 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:UP000184368}.
FT   DOMAIN          345..518
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   662 AA;  73610 MW;  C53BDE9CF494BF32 CRC64;
     MMEYQRKGLS NETLKDLYRR LLWPRLIEEK MLVLLRQGRI SKWFSGIGQE AISVGATAAL
     QQEEWIFPLH RNLGVFTGRG MPLHQLFKQW QGAQDGYSKG RERSFHFGSA DHHVCGMISH
     LGPQLTLANG AALAAKLKGA GKVALAFTGD GGTSEGDFHE ALNVAAVWDL PVIFIIENNG
     YGLSTPVNEQ YRCTQLADRG KGYGMESVTI DGNDILTVYD TIKGVRDYCL QHQKPYLVEC
     MTFRMRGHEE ASGTKYVPKE LFETWAEKDP IKNYETWLLQ EGVMGADETA HIRQSQQQQI
     EAELAMGFQS EPVQVSSEKE LADVYAPHTV KYPLRQVQDT AARSLRFIDA ISEALRQSMD
     WHTNLVLMGQ DIAAYGGAFK ITEGFVQQYG KERVRNTPLC ESAIIGAALG LSLEGYKSMV
     EMQFADFVSV GFNQIVNNLA KIHYRWGQNA DVVIRMPTGG GVGAGPFHSQ SNEAWFVHTP
     GLKVVYPSTP EDAKGLLIAA INDPNPVIYF EHKALYRSIS GPVPEAYYEV EIGKARQVKV
     GEELSIITYG AGVHWAEAFA AEHPEIDLDI LDLRSLLPLD YDAIQASVQR TGKVLLLHED
     TLVGGIGGEL AAWIAEHCFE WLDAPVMRCA SLDTPVPFHT ELEQNFLAKS RLGEVVDRLL
     GY
//