ID A0A0Q7BFU0_9ACTN Unreviewed; 485 AA.
AC A0A0Q7BFU0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KQW48352.1};
GN ORFNames=ASC77_06200 {ECO:0000313|EMBL:KQW48352.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW48352.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW48352.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW48352.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW48352.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW48352.1,
RC ECO:0000313|Proteomes:UP000051939};
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:KQW48352.1}.
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DR EMBL; LMDV01000008; KQW48352.1; -; Genomic_DNA.
DR RefSeq; WP_056150979.1; NZ_LMDV01000008.1.
DR AlphaFoldDB; A0A0Q7BFU0; -.
DR STRING; 1736439.ASC77_06200; -.
DR OrthoDB; 3682986at2; -.
DR Proteomes; UP000051939; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 52..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 485 AA; 50397 MW; F6CC8DE674808C56 CRC64;
MTIDANADQR STTSTPTALP AAHALRGLIG GRVHLPGDAG YDAARLPWNV AIDQRPAAVA
VPRSAAEVAT VVRVAAEAGL RVAPQSTGHN AGPLAAQGLD DVVIVRTSEM NTAIADPVRG
IVRVEGGAIW EPAVDAAAAH GRAVLHGSSP DVGIAGYSLG GGIGWYARKH GLATNSITAV
EIVLADGELV RADAHTNAEL FWAVRGGGGS FGVVTALEFK MFDIATAYAG MMMWPLAAIE
PVLREWAAWA PGAPDEVTTS FRAMRLPELP DLPDFLRGQQ LAVIDGAVLG SDERGCELLA
GLRALDPFLD TFSRVPAKSL VRLHMDPEGG APFASDSAML ASFPDAAVDA FLAEAGPDAQ
TSLLMAELRQ LGGALGRPHQ GGGVLSHLDA QFVTFAGGMA ITPEMGAQAH ADAVRFTEAL
APFANGREYL NFAENPVDTR AAYGADVWTQ LTGIRSAVDP HGVFAANHPV PRLFEDGQAT
SGVRA
//
