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Database: UniProt
Entry: A0A0Q8PJK7_9BURK
LinkDB: A0A0Q8PJK7_9BURK
Original site: A0A0Q8PJK7_9BURK 
ID   A0A0Q8PJK7_9BURK        Unreviewed;       434 AA.
AC   A0A0Q8PJK7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN   ORFNames=ASE07_06655 {ECO:0000313|EMBL:KRB73526.1};
OS   Noviherbaspirillum sp. Root189.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB73526.1, ECO:0000313|Proteomes:UP000051303};
RN   [1] {ECO:0000313|EMBL:KRB73526.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB73526.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB73526.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB73526.1,
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   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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:KRB73526.1}.
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DR   EMBL; LMHZ01000045; KRB73526.1; -; Genomic_DNA.
DR   RefSeq; WP_057292938.1; NZ_LMHZ01000045.1.
DR   AlphaFoldDB; A0A0Q8PJK7; -.
DR   STRING; 1736487.ASE07_06655; -.
DR   OrthoDB; 9781621at2; -.
DR   Proteomes; UP000051303; Unassembled WGS sequence.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF9; TYPE II NADH:QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051303}.
FT   DOMAIN          3..339
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   434 AA;  46803 MW;  732200CF1A18E45B CRC64;
     MHTIVIAGGG AGGLELATRL GDSLGRNGRA RIILIDRSPT HFWKPLLHTV ASGKRDPLMH
     EVAYSAQAAE HGFQFVCGEV LSVDRTRRTV SIGPFRSDDG QEILPARSLR YDKLVLAFGA
     VTNFFNISGA AEHAMTLDSV WQAELFRKRF LANCMHASSR RLAGASEGTI VNIVIVGGGA
     TGVELAAELS HTVRTLAKYN VHTLDPDHDV RVSIVERGEL LLPHLNPRLS RRAARYLRSL
     GVEVCTSTTV ARVDADAVLD TNGTRHAADI TLWAAGVEGP AVCTTLGLPM NRIRQIIVNA
     ALQTPDDDSV YAIGDCSNYI CPVKGAAVPP RAQVAHQQAM YLAEVLAKQP GTRSPDFQYR
     DYGSLVSLGP FAAVGSLLGA APGREMLVGG VTARVLYALM YQKHVMALHG FIRMAAQTVV
     HWLRSKVSPS VKLH
//
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