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Database: UniProt
Entry: A0A0P7YF40_9BACT
LinkDB: A0A0P7YF40_9BACT
Original site: A0A0P7YF40_9BACT 
ID   A0A0P7YF40_9BACT        Unreviewed;       668 AA.
AC   A0A0P7YF40;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:KPQ13164.1};
DE            EC=1.2.4.4 {ECO:0000313|EMBL:KPQ13164.1};
GN   Name=bkdA {ECO:0000313|EMBL:KPQ13164.1};
GN   ORFNames=HLUCCX10_13880 {ECO:0000313|EMBL:KPQ13164.1};
OS   Algoriphagus marincola HL-49.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1305737 {ECO:0000313|EMBL:KPQ13164.1, ECO:0000313|Proteomes:UP000050421};
RN   [1] {ECO:0000313|EMBL:KPQ13164.1, ECO:0000313|Proteomes:UP000050421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-49 {ECO:0000313|EMBL:KPQ13164.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) 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:KPQ13164.1}.
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DR   EMBL; LJXT01000101; KPQ13164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7YF40; -.
DR   STRING; 1305737.GCA_000526355_03757; -.
DR   PATRIC; fig|1305737.6.peg.3485; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG1071; Bacteria.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000050421; Unassembled WGS sequence.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:KPQ13164.1}.
FT   DOMAIN          352..525
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   668 AA;  74838 MW;  26591BC709CB24C7 CRC64;
     MEIATTPSKE LNFDRKKLST TKLLELYEAL IIPRRIEEKM LILLRQGRIS KWFSGWGQEA
     VSVGAVQALM KDEFILPMHR NLGIFTGRKI PLTKLFAQFQ GKKSGFTKGR DRSFHFGSVE
     HHIVGMISHL GPQLAIADGV ALANQLSKEK KVTLVFSGDG ASSEGDFHEG LNVAAVWKLP
     VIFVIEHNGY GLSTPNQEQF AFKNFTDKGP GYGMETVRVE GNNILDVYQT ISDLAKDIRK
     NPRPVLVEAI TFRMRGHEEA SGTKYVPKQV MEEWSKLDPV ENYELYLESL GVLDEKNKEL
     INHKVRKAIT EAWEIAFAEE AILPDLAEEL ADVYAPFDQE VVKPSYGQNC EKRFVDAISD
     GLRQSMEKFP KLVLMGQDIA EYGGVFKITD GFVKEFGADR VRNTPLCESA IIGTGLGLSV
     KGYKAMVEMQ FADFVSVGFN QIVNNLAKIH YRWGQKADLV IRMPTGAGVA AGPFHSQSNE
     AWFFHTPGLK IVYPSNPYDA KGLLNAAIED PNPYLYFEHK ALYRSLSEEI PDDYYTVEIG
     KAKLISEGEQ VSIITYGMGV HWAKKATEEL GLSADILDLR TLLPWDQEAV KSTVKKTGKV
     IFLQEDCLTG GIGAEICAWI SEHCFEYLDA PVMREGSLDT PVPFAPNLEK QFLPEGRFRE
     KLKNLVDF
//
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