ID G9NET8_HYPAI Unreviewed; 452 AA.
AC G9NET8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
DE Flags: Fragment;
GN ORFNames=TRIATDRAFT_4571 {ECO:0000313|EMBL:EHK50819.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK50819.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK50819.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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}.
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:EHK50819.1}.
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DR EMBL; ABDG02000012; EHK50819.1; -; Genomic_DNA.
DR RefSeq; XP_013948950.1; XM_014093475.1.
DR AlphaFoldDB; G9NET8; -.
DR STRING; 452589.G9NET8; -.
DR GeneID; 25784667; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_0_3_1; -.
DR OMA; GETAYEW; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000005426; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:SF14; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000005426}.
FT DOMAIN 9..451
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHK50819.1"
FT NON_TER 452
FT /evidence="ECO:0000313|EMBL:EHK50819.1"
SQ SEQUENCE 452 AA; 49488 MW; E4D8B805328B7C41 CRC64;
DVIVVGGGFS GVMAAYELNQ AGYSVIVLEA KHRIGGRSRS QRLKTNPDAI VELGATWINE
KTQPTIYALT KRFGLKTEAQ HTEGDQIYQG YDGKIYRCDM NQNHNENAQH VQKFVNLLDE
AAEKCNIHTF DEFPEAEDVT MAEWVAQKGL ADNPAVTATC RLLCSAVVGR EPEEIGAHYF
LDYIKSSYGY VSVVSEGDEG AQSLKIKTGT SSIVDALANT LPSGSVMLHS PVDSISQYTD
NEVHVTTSSG TIYKAKKVIM AIPTNTYVNI QFTPPLPSAK KALVTRTKPG VYAKAILTYS
SPWWREVGLL GKFESVIGPI CFSWDVSDIS KKQYSLAIFV AGRVATEWHK LDELAREEAI
IEHLATLVGE TSSLADKARN ILEFNMVEWT KEEYIGGAPT SVLGPGMLKK YGAVLREPVG
NIHFGGGETA YEWKGYMEGA ITAGQRAAKE VV
//