ID A0A084QW05_STAC4 Unreviewed; 704 AA.
AC A0A084QW05;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=S40285_09080 {ECO:0000313|EMBL:KFA68140.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA68140.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA68140.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA68140.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KL659994; KFA68140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QW05; -.
DR STRING; 1283841.A0A084QW05; -.
DR HOGENOM; CLU_014528_0_0_1; -.
DR InParanoid; A0A084QW05; -.
DR OMA; YPCVNNE; -.
DR OrthoDB; 1113861at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.400.10; Acetoacetate decarboxylase-like; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR023375; ADC_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF261; SALICYLATE HYDROXYLASE_MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13860)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF160104; Acetoacetate decarboxylase-like; 1.
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:UP000028524}.
FT DOMAIN 11..367
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 704 AA; 76681 MW; D52ABED954D21CA2 CRC64;
MGATASEEHL NILISGAGIA GLTAALGFRL QGHEVTLFER STAAQETAAA IHLAPNCYGL
LRRFGINPET FGANPVHSIV EYDAQGNLKR DVTLTKALTI WEHPWALAHR ARLHDALKKA
ALDTSGPGFP AVLKTSSRVT KIDCSNASVQ LSDGSWHFGD LVLGADGVSS LTRAAVAGTD
IKPFSSGKSA FRFLVSYGKI RSNTQTERFV KREGCMSLWI GDDRRLVMYP CENNTIMNFV
GIHPSELSLS TNHDGWNSGG SKQVLLDVYR DFGPTVASLL GLVDEKDLKV WTLLDMAQLP
TWVNGKAALL GDAAHPFLPH QGQGGGIAIE DAVSLCALLR RGTRKKDIPD RLALYETIRR
DRAHKVQEYT RIAGTDLNDE NRQTFNIMEF MNYNFGHDEW HNSTHALNKT IWSHDPHSYW
CSPISFGPVA VPLDGQPTQP VDAKTLTYTA RFKASAAYLK TLFPTEAFRF ARPGTVGEIS
FNYTEVEVTT GSGCKHSSVG LSLHGVEYHK VDGSKVVGSF LVVLFESSDD PQSASPVDLG
LPKVYCNIEA VKNDNTLIVT CSSAGNTFLE LSYEELKPVC ETKIVSEEAP VDCSKPGSSG
SPGPLVEEGT LWYRYVPTVG GFGKADAAYP VFAASASPRT PEKAQYIETG TGCNIKFLPG
DWEGFSVVRH VVKGLTEISL YEAVRVTVEK VDGNQDYRKA SKIE
//
