ID   A0A0Q9KIB0_9MICO        Unreviewed;       460 AA.
AC   A0A0Q9KIB0;
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:KRE39208.1};
GN   ORFNames=ASG73_02380 {ECO:0000313|EMBL:KRE39208.1};
OS   Janibacter sp. Soil728.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39208.1, ECO:0000313|Proteomes:UP000051572};
RN   [1] {ECO:0000313|EMBL:KRE39208.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39208.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE39208.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39208.1,
RC   ECO:0000313|Proteomes:UP000051572};
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:KRE39208.1}.
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DR   EMBL; LMRZ01000001; KRE39208.1; -; Genomic_DNA.
DR   RefSeq; WP_055990192.1; NZ_LMRZ01000001.1.
DR   AlphaFoldDB; A0A0Q9KIB0; -.
DR   STRING; 1736393.ASG73_02380; -.
DR   OrthoDB; 5482059at2; -.
DR   Proteomes; UP000051572; 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;
FT   DOMAIN          1..172
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   460 AA;  51815 MW;  CD27565911D7A3D8 CRC64;
     MQTTGWQAHR DAVDRLVRSH DSIPVGSPVR LAKRTSNLFR HRATADVPGL DVSGLAGVIE
     VDPGTRTAQV QGMCTYEDLV AATLPHGLIP LVVPQLRTIT LGGAVTGLGI EATSFRNGLP
     HESVLEMDIL TGSGEVVTAR PDNEHADLFF AFPNSYGSLG YAVRLHIELE AVPPRVALRH
     LRFHDAQSAT DAIDAIVVAG EHEGVRVDAL DGAAFTPDEI YLTLATWTHD ARPTSDYTGQ
     QIYYRSLQER TRDLLTMHDY LWRWDTDWFW CSGAFGVQNP LVRRLWPRRW RRSDVYHRLV
     GLDQRFDIVG RLDARAGRPQ RERVIQDIEV PTERLPEFLA WFDAEVGMRP VWLCPLRLRE
     GPDGIRTWPS YPLDPGRTYV NVGFWGTVHV GDDAPKGPTN RAIETRVHEL GGHKSLYSEA
     FYPRDVFDRL YDGANRAAVQ QRYDPAGRLT DLYDKVVRTL
//