Reviewed, UniProtKB/Swiss-Prot P27338 (AOFB_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 By similarity.
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 59474±14.0 Da from positions 2 - 520. Determined by ESI. Ref.6

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 520

519

Amine oxidase [flavin-containing] B

PRO_0000099859

Regions

Topological domain

2 – 489

488

Cytoplasmic

Transmembrane

490 – 516

27

Anchor for type IV membrane protein

Topological domain

517 – 520

4

Mitochondrial intermembrane

Compositional bias

36 – 52

17

Arg/Lys-rich (basic)

Sites

Site

156

1

Important for catalytic activity

Site

365

1

Important for catalytic activity

Site

382

1

Important for catalytic activity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6

Modified residue

52

1

N6-acetyllysine By similarity

Modified residue

397

1

S-8alpha-FAD cysteine

Experimental info

Mutagenesis

5

1

C → S: No loss of activity. Ref.8

Mutagenesis

156

1

C → S: Complete loss of activity. Ref.8

Mutagenesis

158

1

T → A: Dramatic loss of activity. Ref.7

Mutagenesis

172

1

C → S: No loss of activity. Ref.8

Mutagenesis

192

1

C → S: No loss of activity. Ref.8

Mutagenesis

199

1

I → F: Alters specificity towards synthetic inhibitors.

Mutagenesis

297

1

C → S: No loss of activity. Ref.8

Mutagenesis

312

1

C → S: No loss of activity. Ref.8

Mutagenesis

365

1

C → S: Complete loss of activity. Ref.8

Mutagenesis

382

1

H → R: Significant loss of activity. Ref.7

Mutagenesis

386

1

K → M: No loss of activity. Ref.7

Mutagenesis

389

1

C → A: Complete loss of activity. Ref.8 Ref.7

Mutagenesis

389

1

C → S: No loss of activity. Ref.8 Ref.7

Mutagenesis

394

1

S → A: No loss of activity. Ref.7

Mutagenesis

397

1

C → S: Complete loss of activity. Ref.8

Secondary structure

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520

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

14 – 25

12

Beta strand

30 – 33

4

Beta strand

35 – 40

6

Turn

49 – 51

3

Beta strand

54 – 57

4

Helix

66 – 74

9

Beta strand

79 – 81

3

Beta strand

85 – 92

8

Beta strand

95 – 99

5

Beta strand

101 – 103

3

Helix

109 – 126

18

Helix

134 – 136

3

Helix

140 – 144

5

Beta strand

145 – 147

3

Helix

148 – 155

8

Helix

159 – 173

15

Turn

177 – 179

3

Helix

182 – 190

9

Turn

191 – 193

3

Helix

195 – 199

5

Beta strand

207 – 210

4

Helix

216 – 225

10

Helix

226 – 228

3

Beta strand

235 – 239

5

Beta strand

241 – 249

9

Beta strand

254 – 262

9

Helix

266 – 271

6

Beta strand

272 – 276

5

Helix

280 – 285

6

Beta strand

294 – 300

7

Helix

305 – 309

5

Beta strand

311 – 317

7

Beta strand

325 – 329

5

Beta strand

339 – 345

7

Helix

347 – 352

6

Helix

357 – 372

16

Helix

375 – 378

4

Beta strand

381 – 387

7

Helix

388 – 390

3

Turn

392 – 394

3

Beta strand

396 – 398

3

Helix

406 – 410

5

Helix

411 – 413

3

Beta strand

421 – 423

3

Helix

426 – 428

3

Beta strand

430 – 432

3

Helix

436 – 453

18

Helix

459 – 461

3

Beta strand

470 – 472

3

Helix

481 – 485

5

Helix

489 – 499

11

Sequences

	Sequence		Length	Mass (Da)
	P27338-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 358D1025F5BCA604	FASTA	520	58,763
	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 LLDKLCWTES 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 VLGSLEALEP VHYEEKNWCE EQYSGGCYTT YFPPGILTQY GRVLRQPVDR 430 440 450 460 470 480 IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAQPITTT 490 500 510 520 FLERHLPSVP GLLRLIGLTT IFSATALGFL AHKRGLLVRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human monoamine oxidase A and B genes exhibit identical exon-intron organization." Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C. Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991) [PubMed: 2023912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties." Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W., Seeburg P.H., Shih J.C. Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988) [PubMed: 3387449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical." Chen K., Wu H.F., Shih J.C. J. Neurochem. 61:187-190(1993) [PubMed: 8515265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Promoter organization and activity of human monoamine oxidase (MAO) A and B genes." Zhu Q.S., Grimsby J.S., Chen K., Shih J.C. J. Neurosci. 12:4437-4446(1992) [PubMed: 1432104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[6]	"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.
[7]	"Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis." Cesura A.M., Gottowik J., Lahm H.-W., Lang G., Imhof R., Malherbe P., Roethlisberger U., Da Prada M. Eur. J. Biochem. 236:996-1002(1996) [PubMed: 8665924] [Abstract] Cited for: PROTEIN SEQUENCE OF 371-391, MUTAGENESIS OF THR-158; HIS-382; LYS-386; CYS-389 AND SER-394.
[8]	"Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines." Wu H.F., Chen K., Shih J.C. Mol. Pharmacol. 43:888-893(1993) [PubMed: 8316221] [Abstract] Cited for: MUTAGENESIS OF CYS-5; CYS-156; CYS-172; CYS-192; CYS-297; CYS-312; CYS-365; CYS-389 AND CYS-397.
[9]	"Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders." Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A. Nat. Struct. Biol. 9:22-26(2002) [PubMed: 11753429] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[10]	"Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures." Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A. Proc. Natl. Acad. Sci. U.S.A. 100:9750-9755(2003) [PubMed: 12913124] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
[11]	"Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class." Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A. J. Med. Chem. 47:1767-1774(2004) [PubMed: 15027868] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
[12]	"Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors." Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N., Edmondson D.E. J. Biol. Chem. 280:15761-15766(2005) [PubMed: 15710600] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT PHE-199 IN COMPLEXES WITH INHIBITORS.
[13]	"Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis." Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A. J. Med. Chem. 48:8148-8154(2005) [PubMed: 16366596] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Monoamine oxidase entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

S62734 mRNA. Translation: AAB27229.1.
M69135 Genomic DNA. Translation: AAA59551.1.
M69177 mRNA. Translation: AAA59550.1.
M89637 Genomic DNA. Translation: AAB46386.1.
AL008709, BX537148, Z95125 Genomic DNA. Translation: CAD92552.2.
BX537148, AL008709, Z95125 Genomic DNA. Translation: CAI42422.1.
Z95125, AL008709, BX537148 Genomic DNA. Translation: CAI42522.1.

IPI

IPI00328156.

PIR

JH0817.

RefSeq

NP_000889.3.

UniGene

Hs.654473

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GOS	X-ray	3.00	A/B	1-520	[»]
1H8R	model	-	A	5-459	[»]
1OJ9	X-ray	2.30	A/B	1-520	[»]
1OJA	X-ray	1.70	A/B	1-520	[»]
1OJB	X-ray	2.20	A/B	1-520	[»]
1OJC	X-ray	2.40	A/B	1-520	[»]
1OJD	X-ray	3.10	A/B/C/D/E/F/G/H/I/L	1-520	[»]
1S2Q	X-ray	2.07	A/B	1-520	[»]
1S2Y	X-ray	2.12	A/B	1-520	[»]
1S3B	X-ray	1.65	A/B	1-520	[»]
1S3E	X-ray	1.60	A/B	1-520	[»]
2BK3	X-ray	1.80	A/B	1-520	[»]
2BK4	X-ray	1.90	A/B	1-520	[»]
2BK5	X-ray	1.83	A/B	1-520	[»]
2BYB	X-ray	2.20	A/B	2-519	[»]
2C64	X-ray	2.20	A/B	1-520	[»]
2C65	X-ray	1.70	A/B	1-520	[»]
2C66	X-ray	2.50	A/B	1-520	[»]
2C67	X-ray	1.70	A/B	1-520	[»]
2C70	X-ray	2.06	A/B	2-519	[»]
2C72	X-ray	2.00	A/B	2-519	[»]
2C73	X-ray	2.20	A/B	2-519	[»]
2C75	X-ray	1.70	A/B	2-519	[»]
2C76	X-ray	1.70	A/B	2-519	[»]
2V5Z	X-ray	1.60	A/B	2-519	[»]
2V60	X-ray	2.00	A/B	2-519	[»]
2V61	X-ray	1.70	A/B	2-519	[»]
2VRL	X-ray	2.40	A/B	1-520	[»]
2VRM	X-ray	2.30	A/B	1-520	[»]
2VZ2	X-ray	2.30	A/B	1-520	[»]

ModBase

Search...

PTM databases

PhosphoSite

P27338.

Proteomic databases

PRIDE

P27338.

Genome annotation databases

Ensembl

ENSG00000069535. Homo sapiens. [Contig view]

GeneID

4129.

KEGG

hsa:4129.

NMPDR

fig|9606.3.peg.32658.

Organism-specific databases

GeneCards

GC0XM043510.

H-InvDB

HIX0016741.

HGNC

HGNC:6834. MAOB.

HPA

HPA002328.

MIM

309860. gene.

PharmGKB

PA237.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P27338.

HOVERGEN

P27338.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-32.

BRENDA

1.4.3.4. 247.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.

Reactome

REACT_13433. Biological oxidations.
REACT_649. Phase 1 functionalization.

Gene expression databases

ArrayExpress

P27338.

Bgee

P27338.

CleanEx

HS_MAOB.

GermOnline

ENSG00000069535. Homo sapiens.

Family and domain databases

InterPro

IPR001613. Amineoxid_fl.
IPR002937. Amino_oxidase.
[Graphical view]

Pfam

PF01593. Amino_oxidase. 1 hit.
[Graphical view]

PRINTS

PR00757. AMINEOXDASEF.

ProtoNet

Search...

Other Resources

DrugBank

DB00915. Amantadine.
DB01156. Bupropion.
DB00190. Carbidopa.
DB00215. Citalopram.
DB00988. Dopamine.
DB00494. Entacapone.
DB00614. Furazolidone.
DB01381. Ginkgo biloba.
DB01050. Ibuprofen.
DB00458. Imipramine.
DB04818. Iproniazid.
DB01247. Isocarboxazid.
DB01235. Levodopa.
DB00934. Maprotiline.
DB00737. Meclizine.
DB01171. Moclobemide.
DB00184. Nicotine.
DB01626. Pargyline.
DB00780. Phenelzine.
DB00191. Phentermine.
DB01367. Rasagiline.
DB01037. Selegiline.
DB00752. Tranylcypromine.

NextBio

16210.

SOURCE

Search...

Entry information

Entry name

AOFB_HUMAN

Accession

Primary (citable) accession number: P27338
Secondary accession number(s): Q7Z6S2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)