ID W2YPA3_PHYPR Unreviewed; 470 AA.
AC W2YPA3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=F442_15504 {ECO:0000313|EMBL:ETP36647.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP36647.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP36647.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP36647.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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:ETP36647.1}.
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DR EMBL; ANIY01003284; ETP36647.1; -; Genomic_DNA.
DR AlphaFoldDB; W2YPA3; -.
DR EnsemblProtists; ETP36647; ETP36647; F442_15504.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF405; PEROXISOMAL N(1)-ACETYL-SPERMINE_SPERMIDINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
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|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 13..460
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 470 AA; 51773 MW; 475534F81F5FA5C3 CRC64;
MSEYQVVVIG AGMAGVATAS ALLASNRFKL EDICVLEAQK RIGGRIHTRV FSDELPVKVE
AGAAWIHGTE GNPMIELAQK FGIELEEVSA RNPWLHPSSC PGFLIYEGNR LLSEEEVKET
WEWQDLLLHK IQELALSGEV EGKTLDVVVD GILMEDKELR EVVVSSTNAR ERLALCLHLV
ETWMGSESHE MQIDAFGEID LMGDDPGAHC LVPAGMESFL KHLSAPLKNM IRTNSCVASV
NYEDTNTVVI KCIDGSEVKA DRVVVTCSLG FLKSGKLQFY PELPLSKVDA ISRSQMGQCM
KVMVQFPEAF WPKNASFITQ ISDTTGSEID RVYFPVIFSY YGVKGVPILE GDLIGDKAEA
ISKTLSDDEI ARALFLQLQG MFGIDIPEPV GNLITRWDQD EWARGAYSSV TVDSTYEDPD
LLRQPVASRV FFAGEATNYE HQGALQAAYL SGCHAAAEII TEVSLTINNQ
//
