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Database: UniProt
Entry: A0A0Q8NY45_9BURK
LinkDB: A0A0Q8NY45_9BURK
Original site: A0A0Q8NY45_9BURK 
ID   A0A0Q8NY45_9BURK        Unreviewed;       320 AA.
AC   A0A0Q8NY45;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KRB66341.1};
GN   ORFNames=ASE07_10720 {ECO:0000313|EMBL:KRB66341.1};
OS   Noviherbaspirillum sp. Root189.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB66341.1, ECO:0000313|Proteomes:UP000051303};
RN   [1] {ECO:0000313|EMBL:KRB66341.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB66341.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB66341.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB66341.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRB66341.1}.
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DR   EMBL; LMHZ01000078; KRB66341.1; -; Genomic_DNA.
DR   RefSeq; WP_057293884.1; NZ_LMHZ01000078.1.
DR   AlphaFoldDB; A0A0Q8NY45; -.
DR   STRING; 1736487.ASE07_10720; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000051303; 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:UP000051303}.
FT   DOMAIN          17..311
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   320 AA;  34562 MW;  35A83DD1A1706B5C CRC64;
     MSKITKDGGP VSMLECMMLI RAYEDKVNVM QAAGGGAGTC TSVGQEASAV GVVRALGEDD
     RILTNHRSAG HLLARGADAG RMLAEVMGRS TGYCKGKSGS LHISAKELGV LLTSTIVGGE
     LSLATGVALS KVMLKESGIV ACFFGDGAAC EGIFHESLNL ATVWNLPVLY VCENNQWQAY
     VHRKETMVND HVSEWAKGYG MESRTVDGND VEAVYQATQE AITRIHQTGK PFLLETYTYR
     LRGHFEPDDQ AYVDPAEIAQ WRTRDPIAQL QQRLLARGEI NMADIAQIEA RVAATIEQAA
     AFAQNSPFPD ASELTTDVYA
//
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