ID Q70PK2_CRAGI Unreviewed; 521 AA.
AC Q70PK2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN Name=maoA {ECO:0000313|EMBL:CAD89351.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:CAD89351.1};
RN [1] {ECO:0000313|EMBL:CAD89351.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Digestive gland {ECO:0000313|EMBL:CAD89351.1};
RA Boutet I., Tanguy A., Moraga D.;
RT "Molecular identification and expression of two non-P450 enzymes, monoamine
RT oxidase A and flavin-containing monooxygenase 2, involved in phase I of
RT xenobiotic biotransformation in the Pacific oyster, C rassostrea gigas.";
RL Biochim. Biophys. Acta, Gene Struct. Expr. 1679:29-36(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + serotonin = (5-hydroxyindol-3-yl)acetaldehyde +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:69072, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:50157, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000256|ARBA:ARBA00036170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4(+);
CC Xref=Rhea:RHEA:59416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57887; Evidence={ECO:0000256|ARBA:ARBA00036674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + kynuramine + O2 = 3-(2-aminophenyl)-3-oxopropanal + H2O2
CC + NH4(+); Xref=Rhea:RHEA:59596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:180898,
CC ChEBI:CHEBI:180899; Evidence={ECO:0000256|ARBA:ARBA00036934};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC Evidence={ECO:0000256|ARBA:ARBA00036934};
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:0000256|ARBA:ARBA00000205};
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:0000256|ARBA:ARBA00001138};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004362}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004362}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004362}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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DR EMBL; AJ556989; CAD89351.1; -; mRNA.
DR RefSeq; NP_001292240.1; NM_001305311.1.
DR AlphaFoldDB; Q70PK2; -.
DR SMR; Q70PK2; -.
DR GeneID; 105345865; -.
DR KEGG; crg:105345865; -.
DR CTD; 4128; -.
DR OrthoDB; 5471885at2759; -.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 6.10.250.130; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF11; AMINE OXIDASE [FLAVIN-CONTAINING] A; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 2: Evidence at transcript level;
KW Catecholamine metabolism {ECO:0000256|ARBA:ARBA00022939};
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 18..456
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 521 AA; 58968 MW; DB9C451E64A90BE2 CRC64;
MTMEEDQLVD VIVVGAGLSG LAAAKLLQET GLDVLVLEAR DRVGGRTLTE HNSHVGYVDL
GGAYVGPTQN RLLRLADEFG IKTYFTNEVE DLVFYTKGKS KRYHGAFSPA SGFFEYLDMN
NFFRLLDKMG EEIPPDAPWR APHAKEWDQM TMQQFLDKHV WTKQIYRFCK TFVSVNVTSE
PYEASVLWFL WYIKCCGGQK RIFSTTNGGQ ERKFVGGSQQ ISKRIAEKLG NDRVLLSHPV
CHISQTTDGV TVSVTGGQQF RAKRVIIASP LPLQNKITYD PPLPSLRNQL IQRIPMGSVI
KTFCYYKTPF WKEKGYCGST AIDDDAAIVE FTLDDTKHDG SHPALMGFVL ADKAKRFVSM
TPEEKKESIC RLYAKVFKSD EALYPIHYEE KNWLGEQWSG GCYTAMMPPG FLTNFGEEIR
RPVGNLYFAG TETATQWSGY MEGAVQAGER AAREILFDMK KIPKYEIWQD EEENTLVRAR
PFESTFWERN LPSVGGFLKC VSVTTALAVG SAGLCLYWWK R
//
