ID A3GF87_PICST Unreviewed; 640 AA.
AC A3GF87;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative flavin-containing monooxygenase {ECO:0000313|EMBL:EAZ63308.2};
GN Name=FMO4 {ECO:0000313|EMBL:EAZ63308.2};
GN ORFNames=PICST_28157 {ECO:0000313|EMBL:EAZ63308.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:EAZ63308.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:EAZ63308.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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:EAZ63308.2}.
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; AAVQ01000001; EAZ63308.2; -; Genomic_DNA.
DR RefSeq; XP_001387331.2; XM_001387294.1.
DR AlphaFoldDB; A3GF87; -.
DR GeneID; 4850936; -.
DR KEGG; pic:PICST_28157; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_015676_1_0_1; -.
DR InParanoid; A3GF87; -.
DR OMA; FTHMAYL; -.
DR OrthoDB; 1698450at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43539:SF78; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 4: Predicted;
KW Monooxygenase {ECO:0000313|EMBL:EAZ63308.2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
SQ SEQUENCE 640 AA; 71808 MW; 844DF1A16410E0C2 CRC64;
MTIELSQLVN PPVVSKPVAE DIPPKYIYGT LNPYPEALKV DSLNELASNW IEKFSENLDF
FNEKADKSEA KKSLQTLVAS HASWKDHLAL SWDFRQFHGI DKIREALEKQ AQEFKIKNLK
LRDDAPVKVV TIHEGDPPIE WLQVLFTFEN EYGVGSGAVR LVSTKDENDQ LSLKALSIFT
TLENINGHEE AIGARRSRGL NVGIFNERKL WADERKSQLE YGKSKQPTVL IVGGGQGGLT
VAARLKVMGI DALIVEKNEK IGDNWRNRYD FLVLHDPVWS KHFPYHKYPE SWPEFSPKDK
LGDWFEAYAK NLELNYWTNK EVKNSTFNEE TGTWKVDIVD RSTGNVVALE PSHIVLATGH
SGKPKIPDFK DFNLFQGTVV HAADYKNAGQ IEGKDVVVIG GCNSAIDVAH DLYEQKVKST
IIQRSSTLVI SLEKGVRTTN EGLYDENGPP VEDADLILHS QPIHLLNLLS QQQFRRITSL
EPELNESLEK AGFKTDAGYG ATGLYGKYIR RGGGFYIDVG ACKLISDGEI GLKQGVEIER
FTKDSLVLTD GSEIAASTVI LATGYADMRN TASEIVDEKS NSKLNSVWNL DEEGEVKTIW
RDSGHPNFWF MGGNFLLARY FSKRLALKII ARIEELDKST
//