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Database: UniProt
Entry: F1A178_DICPU
LinkDB: F1A178_DICPU
Original site: F1A178_DICPU 
ID   F1A178_DICPU            Unreviewed;       499 AA.
AC   F1A178;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   ORFNames=DICPUDRAFT_58486 {ECO:0000313|EMBL:EGC30059.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC30059.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC         aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC         ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000205};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362067};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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DR   EMBL; GL871363; EGC30059.1; -; Genomic_DNA.
DR   RefSeq; XP_003293422.1; XM_003293374.1.
DR   AlphaFoldDB; F1A178; -.
DR   STRING; 5786.F1A178; -.
DR   EnsemblProtists; EGC30059; EGC30059; DICPUDRAFT_58486.
DR   GeneID; 10511266; -.
DR   KEGG; dpp:DICPUDRAFT_58486; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; F1A178; -.
DR   OMA; EWTRGAY; -.
DR   OrthoDB; 5471885at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF20; AMINE 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|RuleBase:RU362067};
KW   Membrane {ECO:0000256|RuleBase:RU362067};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Transmembrane {ECO:0000256|RuleBase:RU362067};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT   TRANSMEM        476..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362067"
FT   DOMAIN          16..452
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   499 AA;  56735 MW;  55BD40F503D386D6 CRC64;
     MEESIIHDVV VVGAGLSGLR TSSLLKDENI SVLLLEAQDR VGGRTDSVKI DNYNWDLGGQ
     WVGPTQYRIN ELVKDCNQTT FPQQQKGKKV MEINGTHARY TSLIPPIGLG AVIECQLVVW
     RLDYLSRDLD VTQPWNWKHA EHYDSISMRD WMEDHMYFET SKKLIYISIL AVFSAEPKDI
     SVLFAMTYFK SAGGVSKTIE VEGGAQQDRI YGSSHNISNI LSKKLLIPSA IKIEHDYKTK
     DIIRTTTRNI KTNEECVYLS KYLVLTVPPN IADTIVYQPE LPTIRRQLTK STKMGKVIKF
     IIFYQDCWWR DLGFSGEVVS DRPSISFCYD GSFEDGSKSS IIGFFEGDYA IEWGKKSELE
     RKNEAMAFIY QSFSDDRAFS PTNYLERNWA SNPWSNGGYG CIMGPHDYSN YGKALREPIG
     NIHFAGTETA TEWAGYMEGA LQSAERVSNE IIPKFNSNYK PQLKTNLNGH SNNLNFLNYL
     IMISSMVLIV ILIFYNLLI
//
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