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Protein

Amine oxidase [flavin-containing] B

Gene

MAOB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei156 – 1561Important for catalytic activityBy similarity
Sitei365 – 3651Important for catalytic activityBy similarity
Sitei382 – 3821Important for catalytic activityBy similarity

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.4. 908.
ReactomeiREACT_223515. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.

Names & Taxonomyi

Protein namesi
Recommended name:
Amine oxidase [flavin-containing] B (EC:1.4.3.4)
Alternative name(s):
Monoamine oxidase type B
Short name:
MAO-B
Gene namesi
Name:MAOB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome X

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 489488CytoplasmicBy similarityAdd
BLAST
Transmembranei490 – 51627Helical; Anchor for type IV membrane proteinBy similarityAdd
BLAST
Topological domaini517 – 5204Mitochondrial intermembraneBy similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: Ensembl
  4. mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei397 – 3971S-8alpha-FAD cysteineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP56560.
PRIDEiP56560.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP56560.
SMRiP56560. Positions 3-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 5217Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP56560.
KOiK00274.
OrthoDBiEOG7K6PTP.
TreeFamiTF313314.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKCDVVVV GGGISGMAAA KLLHDSGLNV IVLEARDRVG GRTYTLRNQK
60 70 80 90 100
VKYVDLGGSY VGPTQNHILR LSKELGLETY KVNEVERLIH HTKGKSYPFR
110 120 130 140 150
GSFPSVWNPI TYLDHNNLWR TMDDMGREIP SDAPWKAPLA EQWDLMTMKE
160 170 180 190 200
LLDKICWTES SKQLAILFVN LCVTAEIHEV SALWFLWYVK QCGGTTRIFS
210 220 230 240 250
TSNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIHIDQ TGENVLVETL
260 270 280 290 300
NHELYEAKYV ISAVPPVLGM KIHFNPPLPM MRNQLITRVP LGSVIKSIVY
310 320 330 340 350
YKEPFWRNMD YCGSMIIEGE EAPVAYALDD TKPDGSYPAI IGFILAHKAR
360 370 380 390 400
KLARLTKEER LKKLCDLYAK VLGSQEALHP VHYEEKNWCE EQYSGGCYTS
410 420 430 440 450
YFPPGIMTQY GRVLRQPVGR IYFAGTETAT HWSGYMEGAV EAGERAAREI
460 470 480 490 500
LHAMGKIPED EIWLPEPESV DVPAKPITTT FLQRHLPSVP GLLKLIGLTT
510 520
IFSATALGFL AHKRGLLVRI
Length:520
Mass (Da):58,421
Last modified:January 23, 2007 - v4
Checksum:iA594889B4495C410
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → N in AAF23179 (Ref. 1) Curated
Sequence conflicti270 – 2701M → G AA sequence (PubMed:2719656).Curated
Sequence conflicti286 – 2861I → T in AAF23179 (Ref. 1) Curated
Sequence conflicti297 – 2993SIV → PIM AA sequence (PubMed:2719656).Curated
Sequence conflicti307 – 3071R → K AA sequence (PubMed:2719656).Curated
Sequence conflicti341 – 3411I → L AA sequence (PubMed:2719656).Curated
Sequence conflicti344 – 3441I → K AA sequence (PubMed:2719656).Curated
Sequence conflicti400 – 4001S → A AA sequence (PubMed:2719656).Curated
Sequence conflicti478 – 4858TTTFLQRH → STSSMMMP AA sequence (PubMed:2719656).Curated
Sequence conflicti509 – 5091F → Y in AAI19942 (Ref. 2) Curated
Sequence conflicti520 – 5201I → V in AAF23179 (Ref. 1) Curated

Mass spectrometryi

Molecular mass is 59163.5±10.0 Da from positions 2 - 520. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217955 mRNA. Translation: AAF23179.1.
BC119941 mRNA. Translation: AAI19942.1.
PIRiS07573.
RefSeqiNP_808813.2. NM_177944.2.
UniGeneiBt.22460.

Genome annotation databases

GeneIDi338445.
KEGGibta:338445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217955 mRNA. Translation: AAF23179.1.
BC119941 mRNA. Translation: AAI19942.1.
PIRiS07573.
RefSeqiNP_808813.2. NM_177944.2.
UniGeneiBt.22460.

3D structure databases

ProteinModelPortaliP56560.
SMRiP56560. Positions 3-501.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP56560.
ChEMBLiCHEMBL2756.

Proteomic databases

PaxDbiP56560.
PRIDEiP56560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi338445.
KEGGibta:338445.

Organism-specific databases

CTDi4129.

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP56560.
KOiK00274.
OrthoDBiEOG7K6PTP.
TreeFamiTF313314.

Enzyme and pathway databases

BRENDAi1.4.3.4. 908.
ReactomeiREACT_223515. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.

Miscellaneous databases

NextBioi20812644.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiAOFB_BOVIN
AccessioniPrimary (citable) accession number: P56560
Secondary accession number(s): Q0P5K2, Q864W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 106 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.