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Q5RE98 (AOFB_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Amine oxidase [flavin-containing] B
EC=1.4.3.4
Alternative name(s):
Monoamine oxidase type B
Short name=MAO-B
Gene names
Name:MAOB
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Ontologies

Keywords
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 520519Amine oxidase [flavin-containing] B
PRO_0000099862

Regions

Topological domain2 – 489488Cytoplasmic By similarity
Transmembrane490 – 51627Helical; Anchor for type IV membrane protein; By similarity
Topological domain517 – 5204Mitochondrial intermembrane By similarity
Compositional bias36 – 5217Arg/Lys-rich (basic)

Sites

Site1561Important for catalytic activity By similarity
Site3651Important for catalytic activity By similarity
Site3821Important for catalytic activity By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue521N6-acetyllysine By similarity
Modified residue3971S-8alpha-FAD cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RE98 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D68DC71B2BB6035A

FASTA52058,733
        10         20         30         40         50         60 
MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK VKYVDLGGSY 

        70         80         90        100        110        120 
VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR GPFPPVWNPI TYLDHNNFWR 

       130        140        150        160        170        180 
TMDDMGREIP SDAPWKAPLA EEWDNMTMKE LVDKLCWTES AKQLATLFVN LCVTAETHEV 

       190        200        210        220        230        240 
SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ 

       250        260        270        280        290        300 
TRENVLVETL NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY 

       310        320        330        340        350        360 
YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR KLARLTKEER 

       370        380        390        400        410        420 
LKKLCELYAK VLGSPEALEP VHYEEKNWCE EQYSGGCYTT YFPPGILTQY GRVLRQPVDR 

       430        440        450        460        470        480 
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAQPITTT 

       490        500        510        520 
FLERHLPSVP GLLRLIGLTT IFSATALGFL AHKRGLLVRV

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR857635 mRNA. Translation: CAH89909.1.
RefSeqNP_001124895.1. NM_001131423.1.
UniGenePab.7317.

3D structure databases

ProteinModelPortalQ5RE98.
SMRQ5RE98. Positions 3-501.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171761.
KEGGpon:100171761.

Organism-specific databases

CTD4129.

Phylogenomic databases

HOVERGENHBG004255.
KOK00274.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameAOFB_PONAB
AccessionPrimary (citable) accession number: Q5RE98
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: October 3, 2012
This is version 55 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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