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Database: UniProt
Entry: A0A0Q6VEQ1_9ACTN
LinkDB: A0A0Q6VEQ1_9ACTN
Original site: A0A0Q6VEQ1_9ACTN 
ID   A0A0Q6VEQ1_9ACTN        Unreviewed;       452 AA.
AC   A0A0Q6VEQ1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KQV75231.1};
GN   ORFNames=ASC61_09585 {ECO:0000313|EMBL:KQV75231.1};
OS   Aeromicrobium sp. Root344.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV75231.1, ECO:0000313|Proteomes:UP000051702};
RN   [1] {ECO:0000313|EMBL:KQV75231.1, ECO:0000313|Proteomes:UP000051702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root344 {ECO:0000313|EMBL:KQV75231.1,
RC   ECO:0000313|Proteomes:UP000051702};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV75231.1, ECO:0000313|Proteomes:UP000051702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root344 {ECO:0000313|EMBL:KQV75231.1,
RC   ECO:0000313|Proteomes:UP000051702};
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   -!- 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:KQV75231.1}.
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DR   EMBL; LMDH01000001; KQV75231.1; -; Genomic_DNA.
DR   RefSeq; WP_056211315.1; NZ_LMDH01000001.1.
DR   AlphaFoldDB; A0A0Q6VEQ1; -.
DR   STRING; 1736521.ASC61_09585; -.
DR   OrthoDB; 5482059at2; -.
DR   Proteomes; UP000051702; Unassembled WGS sequence.
DR   GO; GO:0050614; F:delta24-sterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR   InterPro; IPR016170; Cytok_DH_C_sf.
DR   InterPro; IPR040165; Diminuto-like.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR10801; 24-DEHYDROCHOLESTEROL REDUCTASE; 1.
DR   PANTHER; PTHR10801:SF0; DELTA(24)-STEROL REDUCTASE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051702}.
FT   DOMAIN          1..170
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   452 AA;  50546 MW;  E08E67136B616FE9 CRC64;
     MKGWQAHGEA VDRLLASYAR IAPGDRVRLA KKTSNLFRPR QGNDSPGLDV SGLDGVIAID
     TEAQTAEVQG ICTYEQLVAE TLAHGFIPYV VPQLRTITLG GAVTGLGIES TSFRSGLPHE
     SVLEMDILTG SGEVVTAAPE GDHADLFEAF PNSYGSLGYA TRLRIKLEKV PPFVTLRHVQ
     VADAAAAVKA IEVIAETGEW HGERVDGLDG TAFSPDEIYL TLAHFTDTPQ TVSDYTGQQI
     YYRSIQTRET DALTMNDYIW RWDTDWFWCS GAFGAQNRWV RRVWPTRWRR SDVYHRLVGL
     DEKVGLSKVL DRIKKVPGRE RVIQDVEVPV DRLPEFLEWF DAEVGMRPVW LCPLRTTRPW
     PVYPLTPGET YVNAGFWGTV EVPAGSPEGM VNRKIEDFVH SLGGHKSLYS EAFYDQETFE
     QMYGGEVLAA ARGRYDPEGR LSTLYEKAVR NS
//
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