ID A0A0Q7EHM5_9CAUL Unreviewed; 462 AA.
AC A0A0Q7EHM5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASC65_16615 {ECO:0000313|EMBL:KQW86331.1};
OS Brevundimonas sp. Root1279.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW86331.1, ECO:0000313|Proteomes:UP000050923};
RN [1] {ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW86331.1, ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|EMBL:KQW86331.1,
RC ECO:0000313|Proteomes:UP000050923};
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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:KQW86331.1}.
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DR EMBL; LMEB01000002; KQW86331.1; -; Genomic_DNA.
DR RefSeq; WP_056449265.1; NZ_LMEB01000002.1.
DR AlphaFoldDB; A0A0Q7EHM5; -.
DR STRING; 1736443.ASC65_16615; -.
DR OrthoDB; 7592487at2; -.
DR Proteomes; UP000050923; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000050923}.
FT DOMAIN 7..326
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 350..450
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 462 AA; 47811 MW; 69BC2D5A8490D15A CRC64;
MSILSSDVLV IGAGPAGVIA AARAGDLGAR TTLVTSGAFG GMAATDGPAP VRTLAHAARL
MREARQLERY GVTVSPPRLD YPRLLARVDA VVEEVARSSL LRRQIEEAGV AVHAEIGPVH
FVDAHTVETA TGQRFEADKI ILCVGGVSRR LPIPGFELTA THSDAWALTA VPETLIVVGS
GATGAQVASV FNAFGAEVQL FEAGDRIVPT EEPEVSACVA DAFRASGIVV HEAFGAIQSF
EPAPGGVRMT WTKDGARREA VAAVVVIAVG WVADTAAMHL DRAGVGVDAR GFVQVDEAQQ
TTAPHVFAAG DVTGRLMLAP QAQQGGFVAA TNAVTGSRES AARAVNPLGS FTDPEYAQVG
LGEVAARQAH DVEVVAIGFD VTVRAIIDGR TTGLCKLIVD RADHRVLGCH IVGERAVELA
QIAAVVIEAG MTVEALAQLP ISFPTYAGIL GRAAAAAVLK LR
//
