ID A0A0H2LWC5_VARPD Unreviewed; 341 AA.
AC A0A0H2LWC5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acetoin:2,6-dichlorophenolindophenol oxidoreductase subunit alpha {ECO:0000313|EMBL:KLN54533.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:KLN54533.1};
GN Name=acoA {ECO:0000313|EMBL:KLN54533.1};
GN ORFNames=VPARA_41740 {ECO:0000313|EMBL:KLN54533.1};
OS Variovorax paradoxus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN54533.1, ECO:0000313|Proteomes:UP000035170};
RN [1] {ECO:0000313|EMBL:KLN54533.1, ECO:0000313|Proteomes:UP000035170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN54533.1,
RC ECO:0000313|Proteomes:UP000035170};
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-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:KLN54533.1}.
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DR EMBL; JZWI01000022; KLN54533.1; -; Genomic_DNA.
DR RefSeq; WP_021012911.1; NZ_JZWI01000022.1.
DR AlphaFoldDB; A0A0H2LWC5; -.
DR PATRIC; fig|34073.19.peg.4275; -.
DR Proteomes; UP000035170; 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 ECO:0000313|EMBL:KLN54533.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035170}.
FT DOMAIN 45..325
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 341 AA; 35063 MW; 0621DD3C5095BDDF CRC64;
MDPSNSGRSS GTALYRTMVR IRAFENAAET ASQGGVSAYG QQAAGAAKVR GPLHLSTGQE
AVPAGVCAHL RTSDYLTSTH RGHGHTLAKG ADLARMMCEL FGKATGFNGG KGGSMHIADF
SVGMLGANGV VAAGLPIAVG AAHAQKLLRK SDDITVCFFG DGAINRGPFL EALNWARVYA
LPVLFVCEDN RWSATTASGP MTAGDGASAR AASMDIAATQ VDGNDVFAVH ETAARLVAEV
RGGGGPRLLH ALTYRVKGHV SVDLAAYRDP AELAAALETD PIARARGHLL DMGVAAATLD
AIENAARDEV DSALAIAEAA PWPEPGAAFT DVQTTGAGQW T
//