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Database: UniProt
Entry: A0A076N460_AMYME
LinkDB: A0A076N460_AMYME
Original site: A0A076N460_AMYME 
ID   A0A076N460_AMYME        Unreviewed;       465 AA.
AC   A0A076N460;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:AIJ24752.1};
GN   ORFNames=AMETH_4660 {ECO:0000313|EMBL:AIJ24752.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ24752.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ24752.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ24752.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR   EMBL; CP009110; AIJ24752.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A076N460; -.
DR   STRING; 1068978.AMETH_4660; -.
DR   KEGG; amq:AMETH_4660; -.
DR   PATRIC; fig|1068978.7.peg.5009; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_2_3_11; -.
DR   Proteomes; UP000062973; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.300.330; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.3450; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR46568; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR46568:SF1; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 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   FAD {ECO:0000256|PIRSR:PIRSR625650-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR625650-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062973}.
FT   DOMAIN          46..225
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   BINDING         209..215
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   SITE            260
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   465 AA;  49429 MW;  225DD6BA87F82514 CRC64;
     MSESELLIRQ LTAAVGAGKV LTDPAVLSAT SHDTWPVSTK WARQDQHPYR GDVVIRAGSE
     ADVVAVLEVA EETGVPVTTR GLGSSVTGQP LPTRGGIVLD LSGLTGPHEV DEVDMTVTAP
     AGMNGGALED ALNQAGWTMR FSPQSLYRSS VGGWLATLAT GQFSSRYGGV EDLVVGYRVV
     LAGGEVAELT ASPRAAMGPD LRRVFLGSEG TLGVITRVTL KIVPLPAAQH LQTFLVPDVT
     TGLAIMREQA ARGLRPSLLR LYDADEARHA MADPDFDGTV LFVGTEGEPE VAAAEMTVLT
     TMATERGATE LGPEPVQAWL DRRFDFSTVE KRLDTPGGFA ETIEVAHTWR HIEGLYAAIR
     KALEPLADEV LVHFSHVYPQ GTSMYVILLG QVADDAAASA RLAEIWATTM QIGLDHGAEL
     SHHHGGGLAR SPYSRRSLGA AHGVLRRLKH ALDPDGLLNP GKLGL
//
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