ID   A0A1I4S8X3_9FLAO        Unreviewed;       687 AA.
AC   A0A1I4S8X3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:SFM60947.1};
GN   ORFNames=SAMN05421738_101106 {ECO:0000313|EMBL:SFM60947.1};
OS   Algoriella xinjiangensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Algoriella.
OX   NCBI_TaxID=684065 {ECO:0000313|EMBL:SFM60947.1, ECO:0000313|Proteomes:UP000199149};
RN   [1] {ECO:0000313|EMBL:SFM60947.1, ECO:0000313|Proteomes:UP000199149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XJ109 {ECO:0000313|EMBL:SFM60947.1,
RC   ECO:0000313|Proteomes:UP000199149};
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; FOUZ01000001; SFM60947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4S8X3; -.
DR   STRING; 684065.SAMN05421738_101106; -.
DR   Proteomes; UP000199149; 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          353..529
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   687 AA;  76411 MW;  173D1A7E47B6136E CRC64;
     MLTHKFKAMK STLLKQAYEL LVTAKALTEL YEENKQVTGK YVHATSRGHE AIQIATGLQL
     LPQDYLSAYY RDDAMLLAIG ITPYELMLQL LAKRDDVFSG GRTYYSHPSL RRDDMPKIPH
     QSSATGMQAI PTTGIAMGMQ YKELEGLATD EIKPISVCSL GDASCTEGEV AEAFQMAALK
     QLPILYLVQD NEWDISASAD EIRAQDISHY AKGFKGLEVL QVDGTDFLAS YETIQKAIEI
     IRTERRPILV HAKVPLLNHH TSGVRKEWYR DDLEEAQARD PYDKLKTALL NDGFELDELI
     QIEKDAADKV QLEYQEALKA EDPRPEDLYT HVFAPTPITE EKGNRSPEGK EKTVMVDSAL
     FAIRELMAEH PEALLYGQDV GLRLGGVFRE AATLAKQYGK NRVFNTPIQE AFIIGSTVGM
     SAVGLKPIVE VQFADYIWPG LNQLFTEVAR SNYLSNGKWP VSMVLRVPIG AYGSGGPYHS
     SSVESVLTNI KGIKIAYPST GADLKGLMKA AYYDPNPVVM LEHKGLYWSK IKGTEDAATV
     EPDEDYVLPF GKAREVIASE VSTDYNSVSI ITYGMGVYWA KQAAKDFPNQ VEIIDLRTLV
     PLDEETIFTS VKKHSRCIVL TEEAKQNSFA QSVAGLISEE CFEYLDAPVR VLGAQDLPAI
     PLNSTLEQEM LPNAEKLKVL INNVLNY
//