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Database: UniProt
Entry: A7S6X6_NEMVE
LinkDB: A7S6X6_NEMVE
Original site: A7S6X6_NEMVE 
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
//
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