ID F2Q2A3_TRIEC Unreviewed; 435 AA.
AC F2Q2A3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Salicylate hydroxylase {ECO:0000313|EMBL:EGE08271.1};
GN ORFNames=TEQG_07199 {ECO:0000313|EMBL:EGE08271.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; DS995776; EGE08271.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q2A3; -.
DR VEuPathDB; FungiDB:TEQG_07199; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_3_1; -.
DR Proteomes; UP000009169; 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:SF238; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01680)-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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 7..358
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 435 AA; 48420 MW; 9D2D918180A8C5A4 CRC64;
MSSPCFHVAI VGAGLGGLAA AIGIARAGHR VTVLEQQADV QEVGAGIQVP PNASYILQKW
GLLPEVEQVA VRPRDFIVRS YRTGKVLCVQ NAFPYTFERY GVPYLHIHRA DYHRILLNEA
GRLGVDVRLD STVIGIDFDS PAVHLLGKPD FHADLIVGAD GLRSVCRQAL LGHADHPQMT
GDMAYRIIVR GEDVKRHSEL ADLAERPGMT HWIGPNGHAV CYSLKSGEML NLVLVCPDDL
PDTVNLADAD PDEMRTFFQN WDPRLKSLLS LVRETQKWRL RNSGEMDSWS HPSGKFVLLG
DACHATLPYL AQGAAQAIED GAALGTLFER IKDSSQLRDL LSIYEATRKE RTSVIVQSSS
ALRHILHMRD GPGQRNRDTK LYQRSPLESY PIPWIDPKFQ AYLFSYDAFA EASKAWDRYM
NGEDTASKPR VHAHL
//
