AOFB_HUMAN
ID AOFB_HUMAN Reviewed; 520 AA.
AC P27338; B2R6R3; B7Z5H3; D3DWC3; Q7Z6S2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Amine oxidase [flavin-containing] B {ECO:0000305};
DE EC=1.4.3.21 {ECO:0000269|PubMed:11134050, ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:8316221, ECO:0000269|PubMed:8665924};
DE EC=1.4.3.4 {ECO:0000269|PubMed:20493079};
DE AltName: Full=Monoamine oxidase type B;
DE Short=MAO-B;
GN Name=MAOB {ECO:0000312|HGNC:HGNC:6834};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2023912; DOI=10.1073/pnas.88.9.3637;
RA Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.;
RT "Human monoamine oxidase A and B genes exhibit identical exon-intron
RT organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3387449; DOI=10.1073/pnas.85.13.4934;
RA Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W.,
RA Seeburg P.H., Shih J.C.;
RT "cDNA cloning of human liver monoamine oxidase A and B: molecular basis of
RT differences in enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8515265; DOI=10.1111/j.1471-4159.1993.tb03554.x;
RA Chen K., Wu H.F., Shih J.C.;
RT "The deduced amino acid sequences of human platelet and frontal cortex
RT monoamine oxidase B are identical.";
RL J. Neurochem. 61:187-190(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=1432104; DOI=10.1523/jneurosci.12-11-04437.1992;
RA Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.;
RT "Promoter organization and activity of human monoamine oxidase (MAO) A and
RT B genes.";
RL J. Neurosci. 12:4437-4446(1992).
RN [8]
RP PROTEIN SEQUENCE OF 2-17, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=11049757; DOI=10.1006/prep.2000.1309;
RA Newton-Vinson P., Hubalek F., Edmondson D.E.;
RT "High-level expression of human liver monoamine oxidase B in Pichia
RT pastoris.";
RL Protein Expr. Purif. 20:334-345(2000).
RN [9]
RP PROTEIN SEQUENCE OF 371-391, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-158; HIS-382;
RP LYS-386; CYS-389 AND SER-394.
RX PubMed=8665924; DOI=10.1111/j.1432-1033.1996.00996.x;
RA Cesura A.M., Gottowik J., Lahm H.-W., Lang G., Imhof R., Malherbe P.,
RA Roethlisberger U., Da Prada M.;
RT "Investigation on the structure of the active site of monoamine oxidase-B
RT by affinity labeling with the selective inhibitor lazabemide and by site-
RT directed mutagenesis.";
RL Eur. J. Biochem. 236:996-1002(1996).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=20493079; DOI=10.1016/0197-0186(86)90182-8;
RA O'Carroll A.M., Bardsley M.E., Tipton K.F.;
RT "The oxidation of adrenaline and noradrenaline by the two forms of
RT monoamine oxidase from human and rat brain.";
RL Neurochem. Int. 8:493-500(1986).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-5; CYS-156; CYS-172; CYS-192; CYS-297; CYS-312; CYS-365;
RP CYS-389 AND CYS-397.
RX PubMed=8316221;
RA Wu H.F., Chen K., Shih J.C.;
RT "Site-directed mutagenesis of monoamine oxidase A and B: role of
RT cysteines.";
RL Mol. Pharmacol. 43:888-893(1993).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=11134050; DOI=10.1074/jbc.m006972200;
RA Geha R.M., Rebrin I., Chen K., Shih J.C.;
RT "Substrate and inhibitor specificities for human monoamine oxidase A and B
RT are influenced by a single amino acid.";
RL J. Biol. Chem. 276:9877-9882(2001).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14] {ECO:0007744|PDB:1GOS}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH FAD, AND COFACTOR.
RX PubMed=11753429; DOI=10.1038/nsb732;
RA Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A.;
RT "Structure of human monoamine oxidase B, a drug target for the treatment of
RT neurological disorders.";
RL Nat. Struct. Biol. 9:22-26(2002).
RN [15] {ECO:0007744|PDB:1OJ9, ECO:0007744|PDB:1OJA, ECO:0007744|PDB:1OJC, ECO:0007744|PDB:1OJD}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD AND INHIBITORS,
RP AND COFACTOR.
RX PubMed=12913124; DOI=10.1073/pnas.1633804100;
RA Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A.;
RT "Insights into the mode of inhibition of human mitochondrial monoamine
RT oxidase B from high-resolution crystal structures.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9750-9755(2003).
RN [16] {ECO:0007744|PDB:1S2Q, ECO:0007744|PDB:1S2Y, ECO:0007744|PDB:1S3B, ECO:0007744|PDB:1S3E}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH FAD AND INHIBITORS,
RP AND COFACTOR.
RX PubMed=15027868; DOI=10.1021/jm031087c;
RA Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E.,
RA Mattevi A.;
RT "Crystal structures of monoamine oxidase B in complex with four inhibitors
RT of the N-propargylaminoindan class.";
RL J. Med. Chem. 47:1767-1774(2004).
RN [17] {ECO:0007744|PDB:2BK3, ECO:0007744|PDB:2BK4, ECO:0007744|PDB:2BK5}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT PHE-199 IN COMPLEXES WITH
RP FAD AND INHIBITORS, AND COFACTOR.
RX PubMed=15710600; DOI=10.1074/jbc.m500949200;
RA Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N.,
RA Edmondson D.E.;
RT "Demonstration of isoleucine 199 as a structural determinant for the
RT selective inhibition of human monoamine oxidase B by specific reversible
RT inhibitors.";
RL J. Biol. Chem. 280:15761-15766(2005).
RN [18] {ECO:0007744|PDB:2C64, ECO:0007744|PDB:2C65, ECO:0007744|PDB:2C66, ECO:0007744|PDB:2C67}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH FAD AND INHIBITORS,
RP AND COFACTOR.
RX PubMed=16366596; DOI=10.1021/jm0506266;
RA Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E.,
RA Mattevi A.;
RT "Binding of rasagiline-related inhibitors to human monoamine oxidases: a
RT kinetic and crystallographic analysis.";
RL J. Med. Chem. 48:8148-8154(2005).
CC -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC secondary amines such as neurotransmitters, and exogenous amines
CC including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-
CC tetrahydropyridine (MPTP), with concomitant reduction of oxygen to
CC hydrogen peroxide and participates in the metabolism of neuroactive and
CC vasoactive amines in the central nervous system and peripheral tissues
CC (PubMed:11134050, PubMed:8665924, PubMed:8316221, PubMed:11049757,
CC PubMed:20493079). Preferentially degrades benzylamine and
CC phenylethylamine (PubMed:11134050, PubMed:8665924, PubMed:8316221,
CC PubMed:11049757, PubMed:20493079). {ECO:0000269|PubMed:11049757,
CC ECO:0000269|PubMed:11134050, ECO:0000269|PubMed:20493079,
CC ECO:0000269|PubMed:8316221, ECO:0000269|PubMed:8665924}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-adrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde +
CC H2O2 + methylamine; Xref=Rhea:RHEA:51168, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC ChEBI:CHEBI:71406, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:11049757, ECO:0000269|PubMed:11134050,
CC ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:8316221,
CC ECO:0000269|PubMed:8665924};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000305|PubMed:11049757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzylamine + H2O + O2 = benzaldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225238; Evidence={ECO:0000269|PubMed:11049757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC Evidence={ECO:0000305|PubMed:11049757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:27946, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-noradrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde
CC + H2O2 + NH4(+); Xref=Rhea:RHEA:69076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:72587, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225237; Evidence={ECO:0000269|PubMed:11134050,
CC ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:8316221,
CC ECO:0000269|PubMed:8665924};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylputrescine + O2 = 4-acetamidobutanal + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:70283, ChEBI:CHEBI:7386, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58263; Evidence={ECO:0000250|UniProtKB:P19643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70284;
CC Evidence={ECO:0000250|UniProtKB:P19643};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11753429, ECO:0000269|PubMed:12913124,
CC ECO:0000269|PubMed:15027868, ECO:0000269|PubMed:15710600,
CC ECO:0000269|PubMed:16366596};
CC -!- ACTIVITY REGULATION: Inhibited by deprenyl.
CC {ECO:0000269|PubMed:11134050, ECO:0000269|PubMed:20493079}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for 2-phenylethylamine {ECO:0000269|PubMed:11134050};
CC KM=1.92 uM for 2-phenylethylamine {ECO:0000269|PubMed:8316221};
CC KM=2.45 uM for 2-phenylethylamine {ECO:0000269|PubMed:8665924};
CC KM=0.5 mM for 2-benzylamine) {ECO:0000269|PubMed:11049757};
CC KM=0.33 mM for dioxygen {ECO:0000269|PubMed:11049757};
CC KM=226 uM for (R)-adrenaline {ECO:0000269|PubMed:20493079};
CC KM=229 uM for dopamine {ECO:0000269|PubMed:20493079};
CC KM=1093 uM for serotonin {ECO:0000269|PubMed:20493079};
CC KM=238 uM for (R)-noradrenaline {ECO:0000269|PubMed:20493079};
CC KM=4 uM for 2-phenylethylamine {ECO:0000269|PubMed:20493079};
CC KM=107 uM for tyramine {ECO:0000269|PubMed:20493079};
CC Vmax=465 pmol/min/mg enzyme toward (R)-adrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=702 pmol/min/mg enzyme toward dopamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=7 pmol/min/mg enzyme toward serotonin
CC {ECO:0000269|PubMed:20493079};
CC Vmax=321 pmol/min/mg enzyme toward (R)-noradrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=309 pmol/min/mg enzyme toward 2-phenylethylamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=343 pmol/min/mg enzyme toward tyramine
CC {ECO:0000269|PubMed:20493079};
CC -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
CC similar size). Each subunit contains a covalently bound flavin.
CC Enzymatically active as monomer (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P27338; P55212: CASP6; NbExp=3; IntAct=EBI-3911344, EBI-718729;
CC P27338; P28329-3: CHAT; NbExp=3; IntAct=EBI-3911344, EBI-25837549;
CC P27338; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-3911344, EBI-745535;
CC P27338; Q5RI15: COX20; NbExp=3; IntAct=EBI-3911344, EBI-2834035;
CC P27338; Q92915-2: FGF14; NbExp=3; IntAct=EBI-3911344, EBI-12836320;
CC P27338; P22607: FGFR3; NbExp=3; IntAct=EBI-3911344, EBI-348399;
CC P27338; Q53GS7: GLE1; NbExp=3; IntAct=EBI-3911344, EBI-1955541;
CC P27338; P06396: GSN; NbExp=3; IntAct=EBI-3911344, EBI-351506;
CC P27338; P01112: HRAS; NbExp=3; IntAct=EBI-3911344, EBI-350145;
CC P27338; O14901: KLF11; NbExp=3; IntAct=EBI-3911344, EBI-948266;
CC P27338; P13473-2: LAMP2; NbExp=3; IntAct=EBI-3911344, EBI-21591415;
CC P27338; P21397: MAOA; NbExp=2; IntAct=EBI-3911344, EBI-1190845;
CC P27338; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-3911344, EBI-2811583;
CC P27338; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-3911344, EBI-5280197;
CC P27338; P62826: RAN; NbExp=3; IntAct=EBI-3911344, EBI-286642;
CC P27338; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-3911344, EBI-17589229;
CC P27338; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-3911344, EBI-2623095;
CC P27338; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3911344, EBI-5235340;
CC P27338; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-3911344, EBI-741480;
CC P27338; Q9Y649; NbExp=3; IntAct=EBI-3911344, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV
CC membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27338-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27338-2; Sequence=VSP_057047, VSP_057048, VSP_057049;
CC -!- MASS SPECTROMETRY: Mass=59474; Mass_error=14.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11049757};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Monoamine oxidase entry;
CC URL="https://en.wikipedia.org/wiki/Monoamine_oxidase";
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DR EMBL; S62734; AAB27229.1; -; mRNA.
DR EMBL; M69135; AAA59551.1; -; Genomic_DNA.
DR EMBL; AK298942; BAH12909.1; -; mRNA.
DR EMBL; AK312679; BAG35560.1; -; mRNA.
DR EMBL; M69177; AAA59550.1; -; mRNA.
DR EMBL; M89637; AAB46386.1; -; Genomic_DNA.
DR EMBL; AL008709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL020990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471141; EAW59378.1; -; Genomic_DNA.
DR EMBL; CH471141; EAW59380.1; -; Genomic_DNA.
DR CCDS; CCDS14261.1; -. [P27338-1]
DR PIR; JH0817; JH0817.
DR RefSeq; NP_000889.3; NM_000898.4. [P27338-1]
DR PDB; 1GOS; X-ray; 3.00 A; A/B=2-520.
DR PDB; 1OJ9; X-ray; 2.30 A; A/B=2-520.
DR PDB; 1OJA; X-ray; 1.70 A; A/B=2-520.
DR PDB; 1OJC; X-ray; 2.40 A; A/B=2-520.
DR PDB; 1OJD; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/L=2-520.
DR PDB; 1S2Q; X-ray; 2.07 A; A/B=1-520.
DR PDB; 1S2Y; X-ray; 2.12 A; A/B=1-520.
DR PDB; 1S3B; X-ray; 1.65 A; A/B=1-520.
DR PDB; 1S3E; X-ray; 1.60 A; A/B=1-520.
DR PDB; 2BK3; X-ray; 1.80 A; A/B=2-520.
DR PDB; 2BK4; X-ray; 1.90 A; A/B=2-520.
DR PDB; 2BK5; X-ray; 1.83 A; A/B=1-520.
DR PDB; 2BYB; X-ray; 2.20 A; A/B=2-520.
DR PDB; 2C64; X-ray; 2.20 A; A/B=2-520.
DR PDB; 2C65; X-ray; 1.70 A; A/B=2-520.
DR PDB; 2C66; X-ray; 2.50 A; A/B=2-520.
DR PDB; 2C67; X-ray; 1.70 A; A/B=2-520.
DR PDB; 2C70; X-ray; 2.06 A; A/B=2-520.
DR PDB; 2C72; X-ray; 2.00 A; A/B=2-520.
DR PDB; 2C73; X-ray; 2.20 A; A/B=2-520.
DR PDB; 2C75; X-ray; 1.70 A; A/B=2-520.
DR PDB; 2C76; X-ray; 1.70 A; A/B=2-520.
DR PDB; 2V5Z; X-ray; 1.60 A; A/B=2-520.
DR PDB; 2V60; X-ray; 2.00 A; A/B=2-520.
DR PDB; 2V61; X-ray; 1.70 A; A/B=2-520.
DR PDB; 2VRL; X-ray; 2.40 A; A/B=1-520.
DR PDB; 2VRM; X-ray; 2.30 A; A/B=1-520.
DR PDB; 2VZ2; X-ray; 2.30 A; A/B=1-520.
DR PDB; 2XCG; X-ray; 1.90 A; A/B=1-520.
DR PDB; 2XFN; X-ray; 1.60 A; A/B=1-520.
DR PDB; 2XFO; X-ray; 2.10 A; A/B=1-520.
DR PDB; 2XFP; X-ray; 1.66 A; A/B=1-520.
DR PDB; 2XFQ; X-ray; 2.20 A; A/B=1-520.
DR PDB; 2XFU; X-ray; 2.20 A; A/B=2-520.
DR PDB; 3PO7; X-ray; 1.80 A; A/B=1-520.
DR PDB; 3ZYX; X-ray; 2.20 A; A/B=2-520.
DR PDB; 4A79; X-ray; 1.89 A; A/B=1-520.
DR PDB; 4A7A; X-ray; 1.70 A; A/B=1-520.
DR PDB; 4CRT; X-ray; 1.80 A; A/B=1-520.
DR PDB; 5MRL; X-ray; 2.42 A; A/B=1-520.
DR PDB; 6FVZ; X-ray; 1.80 A; A/B=1-520.
DR PDB; 6FW0; X-ray; 1.60 A; A/B=1-520.
DR PDB; 6FWC; X-ray; 1.70 A; A/B=1-520.
DR PDB; 6RKB; X-ray; 2.30 A; A/B=1-520.
DR PDB; 6RKP; X-ray; 1.70 A; A/B=1-520.
DR PDB; 6RLE; X-ray; 2.30 A; A/B=1-520.
DR PDB; 6YT2; X-ray; 1.80 A; A/B=2-520.
DR PDB; 7B0V; X-ray; 2.30 A; A/B=1-520.
DR PDB; 7B0Z; X-ray; 2.10 A; A/B=1-520.
DR PDBsum; 1GOS; -.
DR PDBsum; 1OJ9; -.
DR PDBsum; 1OJA; -.
DR PDBsum; 1OJC; -.
DR PDBsum; 1OJD; -.
DR PDBsum; 1S2Q; -.
DR PDBsum; 1S2Y; -.
DR PDBsum; 1S3B; -.
DR PDBsum; 1S3E; -.
DR PDBsum; 2BK3; -.
DR PDBsum; 2BK4; -.
DR PDBsum; 2BK5; -.
DR PDBsum; 2BYB; -.
DR PDBsum; 2C64; -.
DR PDBsum; 2C65; -.
DR PDBsum; 2C66; -.
DR PDBsum; 2C67; -.
DR PDBsum; 2C70; -.
DR PDBsum; 2C72; -.
DR PDBsum; 2C73; -.
DR PDBsum; 2C75; -.
DR PDBsum; 2C76; -.
DR PDBsum; 2V5Z; -.
DR PDBsum; 2V60; -.
DR PDBsum; 2V61; -.
DR PDBsum; 2VRL; -.
DR PDBsum; 2VRM; -.
DR PDBsum; 2VZ2; -.
DR PDBsum; 2XCG; -.
DR PDBsum; 2XFN; -.
DR PDBsum; 2XFO; -.
DR PDBsum; 2XFP; -.
DR PDBsum; 2XFQ; -.
DR PDBsum; 2XFU; -.
DR PDBsum; 3PO7; -.
DR PDBsum; 3ZYX; -.
DR PDBsum; 4A79; -.
DR PDBsum; 4A7A; -.
DR PDBsum; 4CRT; -.
DR PDBsum; 5MRL; -.
DR PDBsum; 6FVZ; -.
DR PDBsum; 6FW0; -.
DR PDBsum; 6FWC; -.
DR PDBsum; 6RKB; -.
DR PDBsum; 6RKP; -.
DR PDBsum; 6RLE; -.
DR PDBsum; 6YT2; -.
DR PDBsum; 7B0V; -.
DR PDBsum; 7B0Z; -.
DR AlphaFoldDB; P27338; -.
DR SMR; P27338; -.
DR BioGRID; 110302; 65.
DR IntAct; P27338; 24.
DR MINT; P27338; -.
DR STRING; 9606.ENSP00000367309; -.
DR BindingDB; P27338; -.
DR ChEMBL; CHEMBL2039; -.
DR DrugBank; DB08176; (1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINE.
DR DrugBank; DB02211; (R)-N-methyl-N-2-propynyl-1-indanamine.
DR DrugBank; DB08516; (S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE].
DR DrugBank; DB08480; 4-HYDROXY-N-PROPARGYL-1(R)-AMINOINDAN.
DR DrugBank; DB01472; 4-Methoxyamphetamine.
DR DrugBank; DB04307; 5-Hydroxy-N-Propargyl-1(R)-Aminoindan.
DR DrugBank; DB07512; 7-[(3-CHLOROBENZYL)OXY]-2-OXO-2H-CHROMENE-4-CARBALDEHYDE.
DR DrugBank; DB07513; 7-[(3-CHLOROBENZYL)OXY]-4-[(METHYLAMINO)METHYL]-2H-CHROMEN-2-ONE.
DR DrugBank; DB00915; Amantadine.
DR DrugBank; DB00182; Amphetamine.
DR DrugBank; DB06698; Betahistine.
DR DrugBank; DB04889; Bicifadine.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB01363; Ephedra sinica root.
DR DrugBank; DB00668; Epinephrine.
DR DrugBank; DB01175; Escitalopram.
DR DrugBank; DB02509; Farnesol.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB14914; Flortaucipir F-18.
DR DrugBank; DB00614; Furazolidone.
DR DrugBank; DB04818; Iproniazid.
DR DrugBank; DB02095; Isatin.
DR DrugBank; DB01247; Isocarboxazid.
DR DrugBank; DB00601; Linezolid.
DR DrugBank; DB01577; Metamfetamine.
DR DrugBank; DB01442; MMDA.
DR DrugBank; DB01171; Moclobemide.
DR DrugBank; DB08082; N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE.
DR DrugBank; DB02643; N-Dodecyl-N,N-Dimethyl-3-Ammonio-1-Propanesulfonate.
DR DrugBank; DB04677; N-METHYL-N-[(1R)-1-METHYL-2-PHENYLETHYL]PROP-2-EN-1-AMINE.
DR DrugBank; DB03894; N-Propargyl-1(S)-Aminoindan.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB04820; Nialamide.
DR DrugBank; DB00184; Nicotine.
DR DrugBank; DB04821; Nomifensine.
DR DrugBank; DB12612; Ozanimod.
DR DrugBank; DB01626; Pargyline.
DR DrugBank; DB00780; Phenelzine.
DR DrugBank; DB00191; Phentermine.
DR DrugBank; DB00388; Phenylephrine.
DR DrugBank; DB01132; Pioglitazone.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB01168; Procarbazine.
DR DrugBank; DB01367; Rasagiline.
DR DrugBank; DB09363; Rauwolfia serpentina root.
DR DrugBank; DB06654; Safinamide.
DR DrugBank; DB01037; Selegiline.
DR DrugBank; DB01104; Sertraline.
DR DrugBank; DB14569; Tedizolid.
DR DrugBank; DB09042; Tedizolid phosphate.
DR DrugBank; DB00752; Tranylcypromine.
DR DrugBank; DB16446; Vafidemstat.
DR DrugBank; DB04832; Zimelidine.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; P27338; -.
DR GuidetoPHARMACOLOGY; 2490; -.
DR CarbonylDB; P27338; -.
DR GlyGen; P27338; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P27338; -.
DR PhosphoSitePlus; P27338; -.
DR BioMuta; MAOB; -.
DR DMDM; 113980; -.
DR EPD; P27338; -.
DR jPOST; P27338; -.
DR MassIVE; P27338; -.
DR MaxQB; P27338; -.
DR PaxDb; P27338; -.
DR PeptideAtlas; P27338; -.
DR PRIDE; P27338; -.
DR ProteomicsDB; 54379; -. [P27338-1]
DR ProteomicsDB; 6695; -.
DR Antibodypedia; 770; 386 antibodies from 38 providers.
DR DNASU; 4129; -.
DR Ensembl; ENST00000378069.5; ENSP00000367309.4; ENSG00000069535.14. [P27338-1]
DR GeneID; 4129; -.
DR KEGG; hsa:4129; -.
DR MANE-Select; ENST00000378069.5; ENSP00000367309.4; NM_000898.5; NP_000889.3.
DR UCSC; uc004dfz.5; human. [P27338-1]
DR CTD; 4129; -.
DR DisGeNET; 4129; -.
DR GeneCards; MAOB; -.
DR HGNC; HGNC:6834; MAOB.
DR HPA; ENSG00000069535; Tissue enhanced (liver).
DR MIM; 309860; gene.
DR neXtProt; NX_P27338; -.
DR OpenTargets; ENSG00000069535; -.
DR PharmGKB; PA237; -.
DR VEuPathDB; HostDB:ENSG00000069535; -.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000161545; -.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; P27338; -.
DR OMA; PIHWAGT; -.
DR OrthoDB; 1151887at2759; -.
DR PhylomeDB; P27338; -.
DR TreeFam; TF313314; -.
DR BioCyc; MetaCyc:HS00966-MON; -.
DR BRENDA; 1.4.3.4; 2681.
DR PathwayCommons; P27338; -.
DR Reactome; R-HSA-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR SABIO-RK; P27338; -.
DR SignaLink; P27338; -.
DR SIGNOR; P27338; -.
DR BioGRID-ORCS; 4129; 8 hits in 700 CRISPR screens.
DR ChiTaRS; MAOB; human.
DR EvolutionaryTrace; P27338; -.
DR GeneWiki; Monoamine_oxidase_B; -.
DR GenomeRNAi; 4129; -.
DR Pharos; P27338; Tclin.
DR PRO; PR:P27338; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P27338; protein.
DR Bgee; ENSG00000069535; Expressed in saphenous vein and 187 other tissues.
DR Genevisible; P27338; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; TAS:ProtInc.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0097621; F:monoamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:RHEA.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0042420; P:dopamine catabolic process; TAS:ParkinsonsUK-UCL.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; NAS:ParkinsonsUK-UCL.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; IEA:Ensembl.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:Ensembl.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11049757"
FT CHAIN 2..520
FT /note="Amine oxidase [flavin-containing] B"
FT /id="PRO_0000099859"
FT TOPO_DOM 2..489
FT /note="Cytoplasmic"
FT TRANSMEM 490..516
FT /note="Helical; Anchor for type IV membrane protein"
FT TOPO_DOM 517..520
FT /note="Mitochondrial intermembrane"
FT SITE 156
FT /note="Important for catalytic activity"
FT SITE 365
FT /note="Important for catalytic activity"
FT SITE 382
FT /note="Important for catalytic activity"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:11049757"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BW75"
FT MOD_RES 397
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000269|PubMed:11753429,
FT ECO:0000269|PubMed:12913124, ECO:0000269|PubMed:15027868,
FT ECO:0000269|PubMed:15710600, ECO:0000269|PubMed:16366596,
FT ECO:0007744|PDB:1GOS, ECO:0007744|PDB:1OJ9,
FT ECO:0007744|PDB:1OJA, ECO:0007744|PDB:1OJC,
FT ECO:0007744|PDB:1OJD, ECO:0007744|PDB:1S2Q,
FT ECO:0007744|PDB:1S2Y, ECO:0007744|PDB:1S3B,
FT ECO:0007744|PDB:1S3E, ECO:0007744|PDB:2BK3,
FT ECO:0007744|PDB:2BK4, ECO:0007744|PDB:2BK5,
FT ECO:0007744|PDB:2BYB, ECO:0007744|PDB:2C64,
FT ECO:0007744|PDB:2C65, ECO:0007744|PDB:2C66,
FT ECO:0007744|PDB:2C67, ECO:0007744|PDB:2C70,
FT ECO:0007744|PDB:2C72, ECO:0007744|PDB:2C73,
FT ECO:0007744|PDB:2C75, ECO:0007744|PDB:2C76,
FT ECO:0007744|PDB:2V5Z, ECO:0007744|PDB:2V60,
FT ECO:0007744|PDB:2V61, ECO:0007744|PDB:2VRL,
FT ECO:0007744|PDB:2VRM, ECO:0007744|PDB:2VZ2,
FT ECO:0007744|PDB:2XFN, ECO:0007744|PDB:2XFO,
FT ECO:0007744|PDB:2XFP, ECO:0007744|PDB:2XFQ,
FT ECO:0007744|PDB:3PO7, ECO:0007744|PDB:3ZYX,
FT ECO:0007744|PDB:4A79, ECO:0007744|PDB:4A7A,
FT ECO:0007744|PDB:4CRT, ECO:0007744|PDB:5MRL"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /id="VSP_057047"
FT VAR_SEQ 380..427
FT /note="PVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTE ->
FT GSTPASGQDLLCRHRDCHTLERLHGGGCRGRGESSPRDPACHGEDSRG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057048"
FT VAR_SEQ 428..520
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057049"
FT MUTAGEN 5
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 156
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 158
FT /note="T->A: Dramatic loss of activity."
FT /evidence="ECO:0000269|PubMed:8665924"
FT MUTAGEN 172
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 192
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 199
FT /note="I->F: Alters specificity towards synthetic
FT inhibitors."
FT MUTAGEN 297
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 312
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 365
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 382
FT /note="H->R: Significant loss of activity."
FT /evidence="ECO:0000269|PubMed:8665924"
FT MUTAGEN 386
FT /note="K->M: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8665924"
FT MUTAGEN 389
FT /note="C->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221,
FT ECO:0000269|PubMed:8665924"
FT MUTAGEN 389
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221,
FT ECO:0000269|PubMed:8665924"
FT MUTAGEN 394
FT /note="S->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8665924"
FT MUTAGEN 397
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2XFN"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 109..126
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2BYB"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:1S3E"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:1S3E"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6FW0"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 357..372
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1S3E"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 436..453
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:1S3E"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 481..485
FT /evidence="ECO:0007829|PDB:1S3E"
FT HELIX 489..500
FT /evidence="ECO:0007829|PDB:1S3E"
SQ SEQUENCE 520 AA; 58763 MW; 358D1025F5BCA604 CRC64;
MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK VKYVDLGGSY
VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR GPFPPVWNPI TYLDHNNFWR
TMDDMGREIP SDAPWKAPLA EEWDNMTMKE LLDKLCWTES AKQLATLFVN LCVTAETHEV
SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ
TRENVLVETL NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY
YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR KLARLTKEER
LKKLCELYAK VLGSLEALEP VHYEEKNWCE EQYSGGCYTT YFPPGILTQY GRVLRQPVDR
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAQPITTT
FLERHLPSVP GLLRLIGLTT IFSATALGFL AHKRGLLVRV
