ID B6QCC5_TALMQ Unreviewed; 425 AA.
AC B6QCC5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Salicylate hydroxylase, putative {ECO:0000313|EMBL:EEA26580.1};
GN ORFNames=PMAA_076410 {ECO:0000313|EMBL:EEA26580.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA26580.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; DS995900; EEA26580.1; -; Genomic_DNA.
DR RefSeq; XP_002147127.1; XM_002147091.1.
DR AlphaFoldDB; B6QCC5; -.
DR STRING; 441960.B6QCC5; -.
DR VEuPathDB; FungiDB:PMAA_076410; -.
DR HOGENOM; CLU_009665_19_2_1; -.
DR OrthoDB; 1113861at2759; -.
DR PhylomeDB; B6QCC5; -.
DR Proteomes; UP000001294; 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:SF172; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12410)-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:UP000001294}.
FT DOMAIN 15..367
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 425 AA; 47212 MW; 7E030C47AFFE5184 CRC64;
MISKAEPAAW QPLSIAIVGG GIGGLAAGIS LRRAGHTVTI YERANFAGEV GASISCAANG
TRWLHEWGVN VEMGDPVILR KLINRDWETG EAMNVFDLAD YEEKWGHVYN MFHRQYMHAM
LMESAVGEAG EGTPVTLIVN HKCVNIDSAS GLITFANGNT VQHDVIIGAD GIGSVVRGLI
DIHPEKKPST SSCLHTNVTT EEAVALGLID YSQNNAIEYW GGHGTPNKIV LSPCNGGKLL
SYYCFFPREK GDYATQKWDE ESTVEELLAP YPDLDRNVFK HLSIGKDIRP WRLWVHKPYD
WWQKGVVCVM GDAAHPMMPD QSQGACMAIE DAACLGLVFS KEHFRGDIRE ALEVYEKIRK
PRATRVQAAS QRARENIYER IGFSSNTNNE KYTVQDESNK LTIEEMNAYD MKKDVASVFA
NRSKI
//