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Database: UniProt
Entry: A0A166W5I1_9PEZI
LinkDB: A0A166W5I1_9PEZI
Original site: A0A166W5I1_9PEZI 
ID   A0A166W5I1_9PEZI        Unreviewed;       572 AA.
AC   A0A166W5I1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Isoamyl alcohol oxidase (FAD binding domain-containing protein) {ECO:0000313|EMBL:KZL75341.1};
GN   ORFNames=CT0861_03674 {ECO:0000313|EMBL:KZL75341.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL75341.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL75341.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL75341.1,
RC   ECO:0000313|Proteomes:UP000076552};
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 oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:KZL75341.1}.
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DR   EMBL; LFIV01000024; KZL75341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166W5I1; -.
DR   STRING; 708197.A0A166W5I1; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..572
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007881609"
FT   DOMAIN          123..302
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   572 AA;  61291 MW;  82AC66F7CE2E373E CRC64;
     MKSFVLQAAL AGAALAAPNH RLLTGAAVVE RAAADCKCFP GDSCWPATAQ WDTLNTTVGG
     NLIATVPLGS PCHDPTYDAA TCATLQSQWQ QSEIHMESSS SIMAPFFANQ SCDPFQPQSR
     PCLLGNYVVY AVDAKTPEHI QATIAFAQEH NIRFVVRNTG HDYLGRSTGA GALSVWTHHL
     NTAEVVDWNT AAYQGKAMKV GAGTQGFDVM EAAHNAGLAV VGGECPTVGL AGGYTQGGGH
     SALSTSFGLS ADNVLEWEVV IANGTLLTAS KTENVDLFWA LSGGGPGNWG VVTSMTVKAH
     PDAKVGGATL VIMAADNDNT AFFNAIDAFH EELAGMVDGG SMVVYYFAAG FFQIAPLNAY
     NKTADEVKAL LAPFVARLDG LGIKYTVNYS EFESYYNHYD QYFGPLPIGN IQVGIAQYGG
     RLIPRDDITN IGSFSRSVAE KGATFIGVGT DVGKFGNKDT NSVTPAWRNA IVHATLTTVW
     NFTAPWEEML ANQDLMTNVI MKEIEALTPN GGAYMNEADF QQPNFQKEFF GSNYNSLLCL
     KQKWDPEGFF YVRNAVGSES WSVASNGRMC RV
//
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