ID A7S6X6_NEMVE Unreviewed; 519 AA.
AC A7S6X6;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=NEMVEDRAFT_v1g229539 {ECO:0000313|EMBL:EDO40503.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO40503.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO40503.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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:0000256|ARBA:ARBA00035873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70284;
CC Evidence={ECO:0000256|ARBA:ARBA00035873};
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=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:0000256|ARBA:ARBA00036746};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC Evidence={ECO:0000256|ARBA:ARBA00036746};
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; DS469590; EDO40503.1; -; Genomic_DNA.
DR RefSeq; XP_001632566.1; XM_001632516.1.
DR AlphaFoldDB; A7S6X6; -.
DR STRING; 45351.A7S6X6; -.
DR EnsemblMetazoa; EDO40503; EDO40503; NEMVEDRAFT_v1g229539.
DR GeneID; 5512222; -.
DR KEGG; nve:5512222; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; A7S6X6; -.
DR OMA; YNTGNCT; -.
DR OrthoDB; 5471885at2759; -.
DR PhylomeDB; A7S6X6; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR Gene3D; 6.10.250.130; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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:SF1; AMINE OXIDASE [FLAVIN-CONTAINING] B; 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 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 23..460
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 519 AA; 57707 MW; 1232095CEAF6D7FC CRC64;
MDENHANHTE ELRADIIVIG GGISGLCAAK LLQQGHGVDT LVLEARDRVG GRTETLVDPR
FKYTDLGGAY VGPTQNRILR VAKELGVETY QVFFEGKVSE YLGGSRRFYS GEMSTWNPIA
ILDYYSMVKR IGNMCKQISV DAPWNTPQAL EWDRMTVEEF FEKMCLTNYC KKRMVQIYHD
AMAAEPWNMS LLYYLWYLKS GDGMLRVAGV ENAGQERKFV GGSQQISNKL KERLGDRVIL
NSSVVKIAQD EDHVVVTCEN GKSYKAQYVI SAMPQALLNQ VSFNPPLPAL KNQLIQRIPM
GSVIKTITFY DKPFWREKGL NGCVIADSES GPVQAGLDDT KPDGSHPALM GFIIGDQALS
MCQMTQEERK KAVCAQYAKI FNCEEALHPC CYIEKNWLAE KYSGGCYVSV VPCGILTKFR
DTLTLPVGRV HFAGTETATI WCGYMDGAVQ AGERAAREIL HKMGKIPSNM INQEEPPSQE
VVAMPCTLTA FERCLPSVPT AVTAILLGGI LIARYLRAI
//