ID A0A167AHZ1_9PEZI Unreviewed; 598 AA.
AC A0A167AHZ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Phenylacetone monooxygenase protein {ECO:0000313|EMBL:KZL80160.1};
GN ORFNames=CI238_08352 {ECO:0000313|EMBL:KZL80160.1};
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:KZL80160.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL80160.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL80160.1,
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 FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:KZL80160.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFIW01001977; KZL80160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167AHZ1; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF8; MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:KZL80160.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
SQ SEQUENCE 598 AA; 68086 MW; A941BB3788EDAA63 CRC64;
MSDVLLPERM RFGDRDAARR FSAPIHNERH VRIICIGAGA SGLLIAYKLQ RHFQRYSLQC
YEKNSSVAGT WFENRYPGCA CDVPSHNYTW SFEPKLDWSA VYPPASEILE YFENFARKYS
LYQYIKLQHQ VIGAYWNSQN DGYDVHVKDA TTGETFIDHC DILINAGGIL NNWKWPAIPG
LSKFKGILLH TANWDDSVSL EGKSVGLIGN GSSGIQVLPA IRGKCKKIVT FVREPTWVSP
VQGLEQHEFS REEKKEFADK PGALLEYRKK IESGLNGQFG IFLKNNKINE DTHAYFTQQM
KEKLKNPFLE SKLIPEWSVG CRRLTPGVNY LESLTKPNVE VVYGEINEVT ERGCICDNGQ
EYPIDILICA TGFDTSFKPR FPLVAPSGEN LQDKWGVTPE SYFGVAVAGF PNYFLMLGPN
CPIGNGPVLS AIEAQADWML KIIDRYQTTN IAKFAPKEEA VRDFIEYKDW FMNKTVWSDP
CRSWYKPRVD GPVVALWPGS TLHYIEAIKE VRWDDLEVKY AGNRFAWLGN GYSQTELDDT
ADWAYYIRDE DDDPPLTTAG KRRLLTKSGT VKDRNIVVYS GKPGETKEAE QRKEMARL
//