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Database: UniProt
Entry: A0REY8_BACAH
LinkDB: A0REY8_BACAH
Original site: A0REY8_BACAH 
ID   A0REY8_BACAH            Unreviewed;       341 AA.
AC   A0REY8;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Acetoin dehydrogenase (TPP-dependent) E1 component alpha subunit {ECO:0000313|EMBL:ABK85781.1};
GN   OrderedLocusNames=BALH_2494 {ECO:0000313|EMBL:ABK85781.1};
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK85781.1, ECO:0000313|Proteomes:UP000000761};
RN   [1] {ECO:0000313|EMBL:ABK85781.1, ECO:0000313|Proteomes:UP000000761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam {ECO:0000313|EMBL:ABK85781.1,
RC   ECO:0000313|Proteomes:UP000000761};
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000485; ABK85781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0REY8; -.
DR   KEGG; btl:BALH_2494; -.
DR   HOGENOM; CLU_029393_5_0_9; -.
DR   Proteomes; UP000000761; Chromosome.
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   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          32..328
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   341 AA;  37318 MW;  E11DDC831F67CDFA CRC64;
     MNKKIGGLDM LKTTESKGNE ITKEQARWMY KKMLEIRKFE DKVHELFAQG MLPGFVHLYA
     GEEAVAVGVC AHLTDSDSIT STHRGHGHCI AKGCDLNGMM AELFGKATGL CKGKGGSMHI
     ADLDKGMLGA NGIVGGGFPL ACGSALTAKY KGTKDVSVCF FGDGANNEGT FHEGVNLAAI
     WKLPVIFIAE NNGYGEATTF EYASSCDSIA DRAKAYNIPG VQVDGKDLLA VYKAAEEAVE
     RARNGDGPTI IECMTYRNYG HFEGEAQTYK TSEEKEEHLN EKDAIVNFRK HLIHEALLTE
     SELVDMEKAV DEAVQRSIEF SENSPYPEDE ELLKDVYVSY K
//
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