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
//