ID AOFN_ASPNG Reviewed; 495 AA. AC P46882; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Monoamine oxidase N; DE Short=MAO-N; DE EC=1.4.3.4; GN Name=maoN; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 165-175. RX PubMed=7770050; DOI=10.1007/bf00293144; RA Schilling B., Lerch K.; RT "Cloning, sequencing and heterologous expression of the monoamine oxidase RT gene from Aspergillus niger."; RL Mol. Gen. Genet. 247:430-438(1995). 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 -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC {ECO:0000305}. 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; L38858; AAA98490.1; -; Genomic_DNA. DR PIR; S55273; S55273. DR PDB; 2VVL; X-ray; 2.45 A; A/B/C/D/E/F/G/H=1-495. DR PDB; 2VVM; X-ray; 1.85 A; A/B=1-495. DR PDB; 3ZDN; X-ray; 2.55 A; A/B/C/D=1-495. DR PDBsum; 2VVL; -. DR PDBsum; 2VVM; -. DR PDBsum; 3ZDN; -. DR AlphaFoldDB; P46882; -. DR SMR; P46882; -. DR PaxDb; 5061-CADANGAP00009588; -. DR VEuPathDB; FungiDB:An12g03290; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1084380; -. DR VEuPathDB; FungiDB:ATCC64974_41670; -. DR VEuPathDB; FungiDB:M747DRAFT_358493; -. DR eggNOG; KOG0029; Eukaryota. DR BRENDA; 1.4.3.4; 518. DR EvolutionaryTrace; P46882; -. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0097621; F:monoamine oxidase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.660.10; -; 2. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. 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:SF1; FLAVIN-CONTAINING MONOAMINE OXIDASE B-RELATED; 1. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; KW Peroxisome. FT CHAIN 1..495 FT /note="Monoamine oxidase N" FT /id="PRO_0000099865" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 493..495 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:2VVM" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 49..60 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 100..108 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 142..157 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:2VVM" FT TURN 163..167 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 188..195 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 201..215 FT /evidence="ECO:0007829|PDB:2VVM" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 224..233 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 238..246 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 247..250 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 254..266 FT /evidence="ECO:0007829|PDB:2VVM" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 271..276 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 286..293 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 298..306 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 310..315 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 316..320 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 324..332 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 339..346 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 348..352 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 353..357 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 359..362 FT /evidence="ECO:0007829|PDB:2VVL" FT STRAND 365..371 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 377..383 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 385..387 FT /evidence="ECO:0007829|PDB:2VVL" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 395..403 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 412..417 FT /evidence="ECO:0007829|PDB:2VVM" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:2VVM" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 437..446 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 452..454 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 457..459 FT /evidence="ECO:0007829|PDB:2VVM" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:2VVM" FT HELIX 467..485 FT /evidence="ECO:0007829|PDB:2VVM" SQ SEQUENCE 495 AA; 55617 MW; 0E614FF09D3C5B3D CRC64; MTSRDGYQWT PETGLTQGVP SLGVISPPTN IEDTDKDGPW DVIVIGGGYC GLTATRDLTV AGFKTLLLEA RDRIGGRSWS SNIDGYPYEM GGTWVHWHQS HVWREITRYK MHNALSPSFN FSRGVNHFQL RTNPTTSTYM THEAEDELLR SALHKFTNVD GTNGRTVLPF PHDMFYVPEF RKYDEMSYSE RIDQIRDELS LNERSSLEAF ILLCSGGTLE NSSFGEFLHW WAMSGYTYQG CMDCLISYKF KDGQSAFARR FWEEAAGTGR LGYVFGCPVR SVVNERDAAR VTARDGREFA AKRLVCTIPL NVLSTIQFSP ALSTERISAM QAGHVNMCTK VHAEVDNKDM RSWTGIAYPF NKLCYAIGDG TTPAGNTHLV CFGTDANHIQ PDEDVRETLK AVGQLAPGTF GVKRLVFHNW VKDEFAKGAW FFSRPGMVSE CLQGLREKHR GVVFANSDWA LGWRSFIDGA IEEGTRAARV VLEELGTKRE VKARL //