UniProt: C3YCA7

Database: UniProt
Entry: C3YCA7_BRAFL

LinkDB:  C3YCA7_BRAFL 
Original site:  C3YCA7_BRAFL

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Ontology (3)   
   GO (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (10)   

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ID   C3YCA7_BRAFL            Unreviewed;       440 AA.
AC   C3YCA7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   ORFNames=BRAFLDRAFT_125122 {ECO:0000313|EMBL:EEN62139.1};
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:EEN62139.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN62139.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN62139.1};
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=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   -!- 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; GG666500; EEN62139.1; -; Genomic_DNA.
DR   RefSeq; XP_002606129.1; XM_002606083.1.
DR   AlphaFoldDB; C3YCA7; -.
DR   STRING; 7739.C3YCA7; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; C3YCA7; -.
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; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:SF14; AMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 2.
DR   PRINTS; PR00757; AMINEOXDASEF.
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}; Membrane {ECO:0000256|RuleBase:RU362067};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Transmembrane {ECO:0000256|RuleBase:RU362067};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT   TRANSMEM        417..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362067"
FT   DOMAIN          19..99
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          226..379
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   440 AA;  48122 MW;  2871C8FE7191CA2E CRC64;
     MTKEGPVESV DVVVVGGGLS GLSSAYHLSK RNSSCRILVL EAKGRVGGRT ETVPLQGAGG
     QDTWDLGGMW VGRTQLHILQ LLQELGLQTY PQYTRGYTVM QLGSAARVAK YRSDSPIPNM
     PLLSLIDVQL FIWKVERMRK QVPPGDPGSC PHAREWDSMT VETFKQKNLW TQAAKDAVDI
     ACWIVYGVDA SRISLLYYLH YTSCAGGLYP LVETTKGSGQ ELKIKAFWRD RDFSGEVVAY
     DRTADVDGCD TGPIQIAYDN TTGNGNPGLV AFMCANYAKQ WASRSIEQRK AAVLKKFAEY
     FGEEANDPLD FAEKDWGTEP YNGGCPISIM GPGVITNFIP ALRRPCGRIH WAGTETASLW
     CGFMNGAVQS GIRAVVEVLS AMSPHLLSEA DRQELVAVPQ EVETPAKEAH RKKGRKVVSA
     LVGVGLVVGT SLAVYYYIKT
//

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