ID A0A0Q7NHX8_9NOCA Unreviewed; 457 AA.
AC A0A0Q7NHX8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KQY34909.1};
GN ORFNames=ASD42_32595 {ECO:0000313|EMBL:KQY34909.1};
OS Nocardia sp. Root136.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1736458 {ECO:0000313|EMBL:KQY34909.1, ECO:0000313|Proteomes:UP000051507};
RN [1] {ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|Proteomes:UP000051507};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY34909.1, ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|EMBL:KQY34909.1,
RC ECO:0000313|Proteomes:UP000051507};
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|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:KQY34909.1}.
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DR EMBL; LMFE01000004; KQY34909.1; -; Genomic_DNA.
DR RefSeq; WP_056817607.1; NZ_LMFE01000004.1.
DR AlphaFoldDB; A0A0Q7NHX8; -.
DR STRING; 1736458.ASD42_32595; -.
DR Proteomes; UP000051507; 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; 3.50.50.60; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 4..296
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 457 AA; 47792 MW; FE082F910B93BC97 CRC64;
MGGRLVVVGA DATGMAAASQ ARRLRDVGEL EIVVFEKGNH SSYSACGIPY WVAGDVPGAD
DLIARSVAEH RARDIDLRMR TEVTEIDPVG RRVLSRDLDT GAQGWTGYDQ LVLATGATPV
RPPLPGIDAE GVYGVQTLDD GQALIDGLES ATGREAVVVG AGYIGVEMAE ALVRRGFEVT
MITRAAEPMS TLDSDMGALV RKAMEGMGIR IIRDVEVTGM RTAADGKVCA VTTADAEYPA
AVVVLGIGVR PATDLARQAG LPLGESDGLL TDLAQRVRGY DDIWAGGDCV EVLDLVSGTL
RHIPLGTHAN KHGQVIGSGV GGGYATFPGV VGTAVSKVCD LEVARTGLGE KDARRAGLQF
HCVTIESTGR AGYFPGAEPM TVKMLAERRT GRLLGVQIVG RDGAAKRIDI AAVALTARMT
VEQVTALDLG YAPPFSPVWD PVLVAARAAV RAVAEGR
//
