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Protein

Monoamine oxidase N

Gene

maoN

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.

Cofactori

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Monoamine oxidase N (EC:1.4.3.4)
Short name:
MAO-N
Gene namesi
Name:maoN
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Peroxisome Curated

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Monoamine oxidase NPRO_0000099865Add
BLAST

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Turni11 – 133Combined sources
Beta strandi14 – 174Combined sources
Beta strandi26 – 294Combined sources
Beta strandi40 – 456Combined sources
Helixi49 – 6012Combined sources
Beta strandi65 – 684Combined sources
Beta strandi70 – 756Combined sources
Beta strandi80 – 834Combined sources
Beta strandi86 – 894Combined sources
Helixi100 – 1089Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 15716Combined sources
Beta strandi159 – 1624Combined sources
Turni163 – 1675Combined sources
Helixi180 – 1845Combined sources
Helixi188 – 1958Combined sources
Helixi196 – 1983Combined sources
Helixi201 – 21515Combined sources
Turni219 – 2213Combined sources
Helixi224 – 23310Combined sources
Helixi238 – 2469Combined sources
Beta strandi247 – 2504Combined sources
Helixi254 – 26613Combined sources
Turni267 – 2693Combined sources
Beta strandi271 – 2766Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi286 – 2938Combined sources
Beta strandi298 – 3069Combined sources
Helixi310 – 3156Combined sources
Beta strandi316 – 3205Combined sources
Helixi324 – 3329Combined sources
Beta strandi339 – 3468Combined sources
Helixi348 – 3525Combined sources
Beta strandi353 – 3575Combined sources
Beta strandi359 – 3624Combined sources
Beta strandi365 – 3717Combined sources
Beta strandi377 – 3837Combined sources
Helixi385 – 3873Combined sources
Turni391 – 3933Combined sources
Helixi395 – 4039Combined sources
Beta strandi412 – 4176Combined sources
Turni420 – 4223Combined sources
Turni424 – 4263Combined sources
Beta strandi427 – 4304Combined sources
Helixi437 – 44610Combined sources
Beta strandi452 – 4543Combined sources
Helixi457 – 4593Combined sources
Beta strandi461 – 4633Combined sources
Helixi467 – 48519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VVLX-ray2.45A/B/C/D/E/F/G/H1-495[»]
2VVMX-ray1.85A/B1-495[»]
3ZDNX-ray2.55A/B/C/D1-495[»]
ProteinModelPortaliP46882.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46882.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi493 – 4953Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Phylogenomic databases

eggNOGiCOG1231.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

P46882-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSRDGYQWT PETGLTQGVP SLGVISPPTN IEDTDKDGPW DVIVIGGGYC
60 70 80 90 100
GLTATRDLTV AGFKTLLLEA RDRIGGRSWS SNIDGYPYEM GGTWVHWHQS
110 120 130 140 150
HVWREITRYK MHNALSPSFN FSRGVNHFQL RTNPTTSTYM THEAEDELLR
160 170 180 190 200
SALHKFTNVD GTNGRTVLPF PHDMFYVPEF RKYDEMSYSE RIDQIRDELS
210 220 230 240 250
LNERSSLEAF ILLCSGGTLE NSSFGEFLHW WAMSGYTYQG CMDCLISYKF
260 270 280 290 300
KDGQSAFARR FWEEAAGTGR LGYVFGCPVR SVVNERDAAR VTARDGREFA
310 320 330 340 350
AKRLVCTIPL NVLSTIQFSP ALSTERISAM QAGHVNMCTK VHAEVDNKDM
360 370 380 390 400
RSWTGIAYPF NKLCYAIGDG TTPAGNTHLV CFGTDANHIQ PDEDVRETLK
410 420 430 440 450
AVGQLAPGTF GVKRLVFHNW VKDEFAKGAW FFSRPGMVSE CLQGLREKHR
460 470 480 490
GVVFANSDWA LGWRSFIDGA IEEGTRAARV VLEELGTKRE VKARL
Length:495
Mass (Da):55,617
Last modified:November 1, 1995 - v1
Checksum:i0E614FF09D3C5B3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38858 Genomic DNA. Translation: AAA98490.1.
PIRiS55273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38858 Genomic DNA. Translation: AAA98490.1.
PIRiS55273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VVLX-ray2.45A/B/C/D/E/F/G/H1-495[»]
2VVMX-ray1.85A/B1-495[»]
3ZDNX-ray2.55A/B/C/D1-495[»]
ProteinModelPortaliP46882.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1231.

Miscellaneous databases

EvolutionaryTraceiP46882.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger."
    Schilling B., Lerch K.
    Mol. Gen. Genet. 247:430-438(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 165-175.

Entry informationi

Entry nameiAOFN_ASPNG
AccessioniPrimary (citable) accession number: P46882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.