ID   A0A1M3Q916_9PROT        Unreviewed;       334 AA.
AC   A0A1M3Q916;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Acetoin dehydrogenase {ECO:0000313|EMBL:OJY76156.1};
GN   ORFNames=BGP12_01250 {ECO:0000313|EMBL:OJY76156.1};
OS   Rhodospirillales bacterium 70-18.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX   NCBI_TaxID=1895826 {ECO:0000313|EMBL:OJY76156.1, ECO:0000313|Proteomes:UP000184399};
RN   [1] {ECO:0000313|EMBL:OJY76156.1, ECO:0000313|Proteomes:UP000184399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-18 {ECO:0000313|EMBL:OJY76156.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJY76156.1}.
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DR   EMBL; MKWE01000009; OJY76156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3Q916; -.
DR   STRING; 1895826.BGP12_01250; -.
DR   Proteomes; UP000184399; 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}.
FT   DOMAIN          22..316
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   334 AA;  34597 MW;  03C40AACAFBCF3A0 CRC64;
     MPPDQSSRNF DVSRLREQHR LMWRIRALEQ AALRGLAEKV VLGAIHPSIG QEAVAAGVVG
     NLRRDDILLS THRGHGHTLA KGADSEAMLR ELLGRVGGTC GGKGGSMHIA DFQVGMLGAN
     GVVGANIVIA AGAAHAIKLR REDRVVCCIF GDGAINRGPF LEGLNWAAVF GLPVLFVCED
     NGFAATTRTA SMTAGAGPAT RARAFGIVAE EVDGNDILAV DAAVQGLLAQ VRGGGGPRFL
     HASTYRLTGH TGADAAPYRP AEEVAARRLE EPIGRAAELL RGAGVDAAAL AADQAAAEAE
     IAAAYEAAFA APYPEAAEAF RDVQDVGSPL QGAF
//