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Database: UniProt
Entry: A0A0W8DW12_PHYNI
LinkDB: A0A0W8DW12_PHYNI
Original site: A0A0W8DW12_PHYNI 
ID   A0A0W8DW12_PHYNI        Unreviewed;       984 AA.
AC   A0A0W8DW12;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Polyamine oxidase 4 {ECO:0000313|EMBL:KUG00546.1};
GN   ORFNames=AM587_10014757 {ECO:0000313|EMBL:KUG00546.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUG00546.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUG00546.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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:KUG00546.1}.
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DR   EMBL; LNFO01000633; KUG00546.1; -; Genomic_DNA.
DR   STRING; 4790.A0A0W8DW12; -.
DR   EnsemblProtists; KUG00546; KUG00546; AM587_10014757.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF405; PEROXISOMAL N(1)-ACETYL-SPERMINE_SPERMIDINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 2.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..465
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          477..600
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          689..957
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   984 AA;  110773 MW;  6BA4DB6961BBF04C CRC64;
     MAVKSTIDLK SSYRVVVVGA GMAGVSVANA LLVSNEFAAS DVCVLEAQSR IGGRIRTQPF
     SDSLPVNVEV GAAWIHGTEG NPFTDMAKKF GIVFKEVAPR NPWLHPGACK NFLFFDGDKQ
     LPQEQVDETW QWQDLLMHKL QALATSPNAA DHQEKALSAI VDHLVASDEE LGEAMKAPNA
     RARLDMCLKL IEVWMGVNDD EVQLDDFTDI ELIGDDAGAH CIVPAGMEHF IDHLAEPVKE
     SIHTNVVVTS INYEDKDGVV IECSDGRRVS ADHVVVTSSL GFLKSGKLHF QPELPAAKLG
     AIERSKMGQY MKILVEFPEI FWPENSTFIA QIKNSSVSSD AMDRRIYFPV VFNYQFAKGV
     PIIEGVLVGE NASKISATFT EEEIAHALFL QLQETFGPNI PRPVNHFITR WDXDPWSIGA
     YSSLTVDSTD EDPAILRQTV ANRVLFAGEA TDYKYQGALQ AAYLSDSSDG RHIYFPLVFN
     YHLAKGVPIL EGVLIGDNAS AISASFTDEE IAHALFLQMQ ETFGPAVPKP INHFITRWDQ
     DQWSVGAYSC VTARNAHEDP DLLKQTVANR VLFAGEAVDP KYQGALQAAY FTGLEAAAEL
     VTQNLRSRSY QMSCVASDSL QARLRRGEVP CRGVNLGGWL VAEHWMTWDS CLWHGVPDAI
     KNQGEFATMK FLGHEEGDRR FDEHRRSWIT EYDIAEMKRF GLNTVRVPVG YWIMGFDPTD
     FPNKQEWTVF APHSLRYLDE LVNHWCVKYD MAVIVDIHAA KGSQNGRDHS AAVDSGVKYW
     GQYPENVDNT VYLAKFLASR YRFCPSFLGI GLLNEPEHPT EQHVLRAYYE RAYSEIRATG
     NDCVLTVAPL LTEQSPPFME DFMRYPKYFN VWHEWHPYFI WGYEGQNREQ VLQAVRRYGD
     QISSWSGNWL LIDEWSLGAQ GCAFPSEDRY GLQQFASAQL EAFSKAHSGW IFWSWRHSDD
     GHNRPTGWSM RQLLRDGVMR LYDV
//
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