ID   A0A1S8B981_9PEZI        Unreviewed;       485 AA.
AC   A0A1S8B981;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=3-hydroxybenzoate 6-hydroxylase 1 {ECO:0000313|EMBL:OMP83926.1};
GN   ORFNames=BK809_0001309 {ECO:0000313|EMBL:OMP83926.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP83926.1, ECO:0000313|Proteomes:UP000190776};
RN   [1] {ECO:0000313|EMBL:OMP83926.1, ECO:0000313|Proteomes:UP000190776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F98.1 {ECO:0000313|EMBL:OMP83926.1,
RC   ECO:0000313|Proteomes:UP000190776};
RA   Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA   Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT   "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT   in grapevine trunk diseases.";
RL   Submitted (JAN-2017) 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:OMP83926.1}.
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DR   EMBL; MSZU01000106; OMP83926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8B981; -.
DR   STRING; 420778.A0A1S8B981; -.
DR   OrthoDB; 1422702at2759; -.
DR   Proteomes; UP000190776; Unassembled WGS sequence.
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; MONOOXYGENASE; 1.
DR   PANTHER; PTHR13789:SF236; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G12060)-RELATED; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190776}.
FT   DOMAIN          27..416
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  53499 MW;  993A742A610ECAEE CRC64;
     MAPQSRPDDP VQPPPSKAQK STKTTTTRVL IIGAGFAGLT AAIECVRHGH HPVTLLEAFP
     RPTTNLVGDI ISFGHNAGRV FRRWPGVEAT LDPICHRSKE LVFNRYDGEH LMTQTWEEGA
     LEEKGGKKFN GHRGEIHRVV WEEAVAVGVD VRCGERVVEY FEGEGEAGVV VEVEVDEVEA
     DAGVEGGGKE KKEKKRKERK RYAADVVLAA DGVRSTARTI VLGQEDKPKS SGYAIWRAWF
     PSDELAKDPL TRHLVVNGDT HTGWLGPDIH FLAASIKNGT SFSWVCTHKD TADVAESWSA
     PGSVDDALAL LSDWSPTVRA IVRHTPSDRL VDWKLVYRDP LPTWVSPGRR IALIGDAAHP
     FLPTSIQGAS QAVEDGVTVA VCLELATSGS GEGKKGDVRE ALLAYERMRY ERVRKAQKTG
     ETTRDRWHKA DFDKVKEQPE AVKLPREEWL LGHDAEAHAY AVYAETVERI RKEEAKGVPD
     VTSLL
//