ID A0A401KM75_ASPAW Unreviewed; 430 AA.
AC A0A401KM75;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=3-hydroxybenzoate 6-hydroxylase {ECO:0000313|EMBL:GCB20359.1};
GN ORFNames=AAWM_03244 {ECO:0000313|EMBL:GCB20359.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB20359.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB20359.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB20359.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:GCB20359.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDHI01000007; GCB20359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KM75; -.
DR STRING; 105351.A0A401KM75; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF307; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04330)-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..355
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 347..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47243 MW; 9260732A1EF449CE CRC64;
MEQAKTPLQV IVVGAGIGGM AAALTLGLRG HHVTILESAP KLMEVGAGIQ VSPNMLTLFD
RWGVSPLIHA QDVALEHIHV RRWEDGSMLG TLPVNKTYGQ QTVIHRADLH NALIEKALAL
SNVELRVNST VTGVQFDHAA VQLANGTIVK GDIVIAADGI KSALRDHLLE EASVAIPTGD
AAYRIMLPRS ALENDPELKA LVDEPQATRW LGPGRHVIAY PVRNHDLYNV VLLHPDSHGV
EESWTTKGSK QAMVDNYKGW DRRVTKLIDL VPDDEVLEWK LCLHAPLKTW IRGSVALIGD
ACHPMLPYVA QGAAQAVEDA AALGVLLSTI SSRDEIPLAL KAYEKSRKPR ADTVQQSGSE
NRITLHLPDG PEQRARDEQF RSSLKSGSNP DRWTDLETQK FLWGWDAEKA ALDAWNELHG
NHVSELRHHL
//
