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Database: UniProt
Entry: A0A0F0H2M1_9ACTN
LinkDB: A0A0F0H2M1_9ACTN
Original site: A0A0F0H2M1_9ACTN 
ID   A0A0F0H2M1_9ACTN        Unreviewed;       539 AA.
AC   A0A0F0H2M1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KJK48517.1};
GN   ORFNames=UK14_18120 {ECO:0000313|EMBL:KJK48517.1};
OS   Streptomyces sp. NRRL F-4428.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK48517.1, ECO:0000313|Proteomes:UP000033569};
RN   [1] {ECO:0000313|EMBL:KJK48517.1, ECO:0000313|Proteomes:UP000033569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK48517.1,
RC   ECO:0000313|Proteomes:UP000033569};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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:KJK48517.1}.
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DR   EMBL; JYJI01000141; KJK48517.1; -; Genomic_DNA.
DR   RefSeq; WP_045322736.1; NZ_JYJI01000141.1.
DR   AlphaFoldDB; A0A0F0H2M1; -.
DR   PATRIC; fig|1609137.3.peg.4068; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000033569; Unassembled WGS sequence.
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   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:UP000033569}.
FT   DOMAIN          98..280
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          358..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        459
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         131..137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         264..270
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            315
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   539 AA;  56855 MW;  DFD689329E89DAAA CRC64;
     MPGTRPQPTP ATRTRSWWGW GWSDAHPGDA ECAAMGALVP GTLAHPLPVP RVRDLDIERP
     AVQPPAGLAH LVSTAPEERA AHAMGKAYRD VVRALRGRPG RIPDLVARPT DEREVADLLD
     WAGERQVAVV PYGGGSSVSG GVEYRGDAHD AVLSLDLTAM DRVLEVDAVG RAARIQAGAL
     GPGLEDQLRP HGLTLRHFPQ SFEFSTLGGW LATRAGGHYA TGRTHIDDFV QSLRVVTPAG
     TSASWRLPAS GAGPSPDRLF LGSEGALGVI TEAWVRLQER PAHKASASLA FTDFHAALEA
     VRALAQSDLS PANCRLLDAG EAALSGASHD GSAVLVLGFE SADGPVTARL GQAVDLARSH
     GGRHGGRHGD PGGTGGADDD AAVSAWRSAF LRMPYLRDGL ARMGAVAETF ETAATWDRIP
     GLIEAVRTEV GEAALKASGH PAIVNCRLTH VYPDGAAPYF TVLAGGRPGD EVAFWDDLKA
     VASDVLHRHR ATITHHHAVG RDHRPGYDRQ RPDPFALALR AAKGALDPRG ILNPGVLVD
//
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