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Database: UniProt
Entry: H0BZR2_9BURK
LinkDB: H0BZR2_9BURK
Original site: H0BZR2_9BURK 
ID   H0BZR2_9BURK            Unreviewed;       318 AA.
AC   H0BZR2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=TPP-dependent acetoin dehydrogenase complex, E1 component subunit alpha {ECO:0000313|EMBL:EHL22135.1};
GN   ORFNames=KYG_14493 {ECO:0000313|EMBL:EHL22135.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL22135.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL22135.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL22135.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; AGTS01000087; EHL22135.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0BZR2; -.
DR   STRING; 512030.KYG_14493; -.
DR   PATRIC; fig|512030.4.peg.2856; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000003485; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485}.
FT   DOMAIN          34..309
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   318 AA;  33491 MW;  05B4028CEE9634DD CRC64;
     MYRNMVTSRK FEETIAKIYF EGKLPVFSMA DGPIPGEMHL SDGQEPVAVG VCAHLEASDI
     VTATHRPHHQ AIAKGVDLDK MAAEIFGKAT GLSGGRGGHM HLFDPKVNFA CSGIIAQGMG
     PAVGAALSRK MQKKPGVAVA FVGEGAVNQG GWHEAMNLAA TWKLPFICVI EDNAWGISVS
     KEASTAISNN ADRAAAYGIP GKRIAGNDPY AIYEAAGEAI ARARAGEGPS LLEIETYRLA
     GHFMGDAEGY RPKGEKDALF AKDPIPKMRA KMIADGVATG AELDAIEAQA AARVEQAIKF
     ARESADPAPE TALTSVFA
//
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