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Reviewed, UniProtKB/Swiss-Prot P56560 (AOFB_BOVIN)

Last modified November 25, 2008. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

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

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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

RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2).

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

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Ontologies

Keywords

   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionamine oxidase activity

Inferred from electronic annotation. Source: EC

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Topological domain2 – 489488Cytoplasmic By similarity
Transmembrane490 – 51627Anchor 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
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

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Sequences

Sequence LengthMass (Da)Tools
P56560-1 [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

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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: 11049757] [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: 2719656] [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: 2764901] [Abstract]
Cited for: DETERMINATION OF PROTEIN-FAD RATIO.
Tissue: Liver.

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Cross-references

Sequence databases

AF217955 mRNA. Translation: AAF23179.1.
BC119941 mRNA. Translation: AAI19942.1.
PIRS07573.
RefSeqNP_808813.2.
UniGeneBt.22460

3D structure databases

HSSPHSSP built from PDB template 1GOS based on UniProtKB P27338.
SMRP56560. Positions 3-501.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000001288. Bos taurus. [Contig view]
GeneID338445.
KEGGbta:338445.

Phylogenomic databases

HOVERGENP56560.

Family and domain databases

InterProIPR001613. Amineoxid_fl.
IPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

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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: November 25, 2008
This is version 60 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents