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P56560 (AOFB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

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

Subunit structure

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

Subcellular location

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

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Mass spectrometry

Molecular mass is 59163.5±10.0 Da from positions 2 - 520. Determined by ESI. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 520519Amine oxidase [flavin-containing] B
PRO_0000099856

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 Ref.3
Modified residue521N6-acetyllysine By similarity
Modified residue3971S-8alpha-FAD cysteine By similarity

Experimental info

Sequence conflict31S → N in AAF23179. Ref.1
Sequence conflict2701M → G AA sequence Ref.4
Sequence conflict2861I → T in AAF23179. Ref.1
Sequence conflict297 – 2993SIV → PIM AA sequence Ref.4
Sequence conflict3071R → K AA sequence Ref.4
Sequence conflict3411I → L AA sequence Ref.4
Sequence conflict3441I → K AA sequence Ref.4
Sequence conflict4001S → A AA sequence Ref.4
Sequence conflict478 – 4858TTTFLQRH → STSSMMMP AA sequence Ref.4
Sequence conflict5091F → Y in AAI19942. Ref.2
Sequence conflict5201I → V in AAF23179. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P56560 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: A594889B4495C410

FASTA52058,421
        10         20         30         40         50         60 
MSSKCDVVVV GGGISGMAAA KLLHDSGLNV IVLEARDRVG GRTYTLRNQK VKYVDLGGSY 

        70         80         90        100        110        120 
VGPTQNHILR LSKELGLETY KVNEVERLIH HTKGKSYPFR GSFPSVWNPI TYLDHNNLWR 

       130        140        150        160        170        180 
TMDDMGREIP SDAPWKAPLA EQWDLMTMKE LLDKICWTES SKQLAILFVN LCVTAEIHEV 

       190        200        210        220        230        240 
SALWFLWYVK QCGGTTRIFS TSNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIHIDQ 

       250        260        270        280        290        300 
TGENVLVETL NHELYEAKYV ISAVPPVLGM KIHFNPPLPM MRNQLITRVP LGSVIKSIVY 

       310        320        330        340        350        360 
YKEPFWRNMD YCGSMIIEGE EAPVAYALDD TKPDGSYPAI IGFILAHKAR KLARLTKEER 

       370        380        390        400        410        420 
LKKLCDLYAK VLGSQEALHP VHYEEKNWCE EQYSGGCYTS YFPPGIMTQY GRVLRQPVGR 

       430        440        450        460        470        480 
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWLPEPESV DVPAKPITTT 

       490        500        510        520 
FLQRHLPSVP GLLKLIGLTT IFSATALGFL AHKRGLLVRI

« Hide

References

« Hide 'large scale' references
[1]Chung P.P., Vaidyanathan G., Lanier S.M.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Basal ganglia.
[3]"High-level expression of human liver monoamine oxidase B in Pichia pastoris."
Newton-Vinson P., Hubalek F., Edmondson D.E.
Protein Expr. Purif. 20:334-345(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[4]"The primary structure of bovine monoamine oxidase type A. Comparison with peptide sequences of bovine monoamine oxidase type B and other flavoenzymes."
Powell J.F., Hsu Y.-P.P., Weyler W., Chen S.A., Salach J., Andrikopoulos K., Mallet J., Breakefield X.O.
Biochem. J. 259:407-413(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-36; 53-70; 101-120; 259-279; 289-323; 327-346; 362-403; 420-431 AND 456-485.
[5]"Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit."
Weyler W.
Biochem. J. 260:725-729(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DETERMINATION OF PROTEIN-FAD RATIO.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF217955 mRNA. Translation: AAF23179.1.
BC119941 mRNA. Translation: AAI19942.1.
IPIIPI00705282.
PIRS07573.
RefSeqNP_808813.2. NM_177944.2.
UniGeneBt.22460.

3D structure databases

ProteinModelPortalP56560.
SMRP56560. Positions 3-501.
ModBaseSearch...

Proteomic databases

PaxDbP56560.
PRIDEP56560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000001698; ENSBTAP00000001698; ENSBTAG00000001288.
GeneID338445.
KEGGbta:338445.

Organism-specific databases

CTD4129.

Phylogenomic databases

eggNOGCOG1231.
GeneTreeENSGT00530000063101.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidP56560.
KOK00274.
OrthoDBEOG412M55.

Enzyme and pathway databases

BRENDA1.4.3.4. 908.

Family and domain databases

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

Other

BindingDBP56560.
ChEMBLCHEMBL2756.
NextBio20812644.

Entry information

Entry nameAOFB_BOVIN
AccessionPrimary (citable) accession number: P56560
Secondary accession number(s): Q0P5K2, Q864W3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 93 of the entry and version 4 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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