ID A0A0Q7B3S1_9ACTN Unreviewed; 457 AA.
AC A0A0Q7B3S1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KQW47331.1};
GN ORFNames=ASC77_12725 {ECO:0000313|EMBL:KQW47331.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW47331.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW47331.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW47331.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW47331.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW47331.1,
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:KQW47331.1}.
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DR EMBL; LMDV01000009; KQW47331.1; -; Genomic_DNA.
DR RefSeq; WP_056154463.1; NZ_LMDV01000009.1.
DR AlphaFoldDB; A0A0Q7B3S1; -.
DR STRING; 1736439.ASC77_12725; -.
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; IPR012951; BBE.
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 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; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 34..205
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 48934 MW; E2F9C78E12DE8B86 CRC64;
MSAQLDTLRE QIRGTVTGPD DPGYDDARTV RNGMIDKRPA VIVQAANAGD VMTAVRFAAD
NAMTVAVRGG AHSVPGFGTA DGAVVVDLSA MRGGRVDPLT QTVRVGGGAT WGDLNAMTYP
FGLATTGGII STTGVGGLTL GGGIGYLSRG LGLSVDNLLA ADVVTADGTF HVASEKEDAD
LFWAIRGGGG NFGVVTSFEF RLSPVKDIYG GPMFFELDRA GDVLRFYRDF IVDAPEELGC
FPAYQIAPPL PFIPEDRHGE PFIAMVACWA GDLDAGEKAL QPIRDVAPRV AEMVGPMPYP
ALNSAFDALI PPGLHHYWKA SFVKELTDDA IAAHLEHGPK VPVVNSTMHI YPINGACHRV
APDATAFAHR DATFATVIAG MWPPDELDDA DGTAWVRDYY DATAPHSEEG GYINFMAEDD
QDRIRANYKG SYDRLQSIKT TYDPDNLFRH NQNIVPA
//
