AOFN_ASPNG
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 25-MAY-2022, entry version 93.
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}.
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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 STRING; 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; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 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
