ID C3ZEL9_BRAFL Unreviewed; 501 AA.
AC C3ZEL9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_277883 {ECO:0000313|EMBL:EEN49175.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN49175.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49175.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN49175.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666612; EEN49175.1; -; Genomic_DNA.
DR RefSeq; XP_002593164.1; XM_002593118.1.
DR AlphaFoldDB; C3ZEL9; -.
DR STRING; 7739.C3ZEL9; -.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; C3ZEL9; -.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR Gene3D; 3.90.660.10; -; 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: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|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067}.
FT DOMAIN 24..459
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT NON_TER 501
FT /evidence="ECO:0000313|EMBL:EEN49175.1"
SQ SEQUENCE 501 AA; 54163 MW; C50882FFFFEF6F8D CRC64;
MASFETGGEK NVVDTDVVVV GAGISGLCAA KLLHETGLDV QVLEARDRVG GRTYTVSHPS
SGYADLGGAY VGTGQDRILR VAKELDLKFY KVNDEGKSVS YMEGVHRSGS ADDPSLLTKN
PLALLDMNNL LWKIDEFSKQ VPPDTPWKAP RAKEWDSMTV KEFMDKECWT SVTKKLLGLL
VATLSCCEPE ELSFLFLLAG VASSGGFGNA ISEAQENKFV GGSMQVSEKI AALLGNRVVL
SSPVMRIEQG EAVTMVTTHS GQQYRAKYVI SAIPPTLLHG ILFEPPLPGL KIQMIQRMPM
GSVIKTMTYY ETAFWKDNLG FSGTAMSDTG PVVACMDDTK PDGSFPALVG FITSTQAKKV
CDMSVEERKQ AVCEHYAEVF QCPEFLHPVH YVEHNWMADT FSGGGPGANL GPGVLTSFGS
ELGKPFGCVY FAGTETAVKW GGYMDGAVEA GERAAREILH AMGKISEDEI WQEEPPSSDV
PSTPGAAISW EKYLPSVPQL L
//