ID A0A2V1E6H7_9PLEO Unreviewed; 438 AA.
AC A0A2V1E6H7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Salicylate hydroxylase {ECO:0000313|EMBL:PVI05742.1};
GN ORFNames=DM02DRAFT_668089 {ECO:0000313|EMBL:PVI05742.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI05742.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI05742.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI05742.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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; KZ805312; PVI05742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1E6H7; -.
DR STRING; 97972.A0A2V1E6H7; -.
DR Proteomes; UP000244855; 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:SF306; HYDROXYLASE, PUTATIVE-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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..438
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016119826"
FT DOMAIN 2..329
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 438 AA; 48152 MW; DFA797F71D1C0344 CRC64;
MKIIIIGAGI AGLSTAIALA HSATEHDIIL LESASRLAEV GAGIQLTAVA TRQFLRWGLG
PELLAVASIP TSWNLRRGSD GSILNRVPFK ELEPTYGGPY VVIHRADLHR ILHRHAVKKG
ARIELNSRVM QYGVEEGWVL LENGVRMQAD LIVACDGINS MAREHLLKYL GEKHEDTVQP
TGWAAYRAMV NVDDVKRDSL IAEIVAEHNG NCWADEDKLL MSYMVRDSGK LNLVFSHRDT
VETGSWTQDQ FLQELRNMSK GMDPRVQRLI NLINAPITNW PVYAIRTLPT WTSKSGRFVL
IGDAAHAMAF YLSMGVSMAV EDAAALAWVV ERSTDSSQAI SLASAMSLFV KVRKPRAELI
RDASLHAAAI LQLPPGPDRD IRDAAAMQDG LVGEASKQGN CLVDWKSYGI ADRTIRDACY
SYDVIADIEE QANTVGSQ
//
