ID A0A162QBI9_9PEZI Unreviewed; 469 AA.
AC A0A162QBI9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Salicylate hydroxylase {ECO:0000313|EMBL:KZL88347.1};
GN ORFNames=CI238_11702 {ECO:0000313|EMBL:KZL88347.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL88347.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL88347.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL88347.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL88347.1}.
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DR EMBL; LFIW01000003; KZL88347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162QBI9; -.
DR STRING; 1573173.A0A162QBI9; -.
DR Proteomes; UP000076584; 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:SF147; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01950)-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:UP000076584}.
FT DOMAIN 33..204
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 469 AA; 51247 MW; BCF44C12588408FC CRC64;
MSEDPVELSS AVCYASEEHY GTSSETMSDP KDLKIAIIGA GMGGLGCALA LAKKGFKHID
VYETASNLGF VGAGIQMPPN VVRVLDRLGC WPDIEKTCTD VKGSSIRQGS TNVELAHVDM
PNIRELYGYP HCNDHRSSLA GGMYDACKKE PAITFHFATA LVSVNSFAPK PNFTVQPRGG
EAHSVESDIL LACDGIKSIV RSSLLDSIGA VGGEEETGQA AYRIMLTREQ MADDPELLAL
LDSDEVVRWI GEKRHIIAYP VSSHTIYNLS TTQPDSNFAA ATNATYTTKG SKKVMLDVFH
DFCPLVHRML NLVPDGEVCE WRLRMHKPLP TWVHTDGPVA LLGDACHPTL PHLSQGAAMA
IEDGSVVAEV LARAPDADPK TLRRCLKAYE LSRRDWTSQL VNMAFLSGKQ LHLGEGKAKE
ERDRMFAEHK SAGAVPDKWA SPDVQRMIYT NDCVANIQRD FDELYKSAA
//