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Database: UniProt
Entry: C3Z117_BRAFL
LinkDB: C3Z117_BRAFL
Original site: C3Z117_BRAFL 
ID   C3Z117_BRAFL            Unreviewed;       634 AA.
AC   C3Z117;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
DE   Flags: Fragment;
GN   ORFNames=BRAFLDRAFT_217434 {ECO:0000313|EMBL:EEN53716.1};
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:EEN53716.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN53716.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN53716.1};
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|RuleBase:RU000672};
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC       ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
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DR   EMBL; GG666571; EEN53716.1; -; Genomic_DNA.
DR   RefSeq; XP_002597704.1; XM_002597658.1.
DR   AlphaFoldDB; C3Z117; -.
DR   STRING; 7739.C3Z117; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   InParanoid; C3Z117; -.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   InterPro; IPR015800; Cu_amine_oxidase_N2.
DR   PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000672};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          1..50
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          222..626
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          208..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        381
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         381
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEN53716.1"
FT   NON_TER         634
FT                   /evidence="ECO:0000313|EMBL:EEN53716.1"
SQ   SEQUENCE   634 AA;  72439 MW;  C6DA21F65EBAA885 CRC64;
     ELYVPAKSEA LAFLDGGGAK PERQALVTVH AGGKTPPVVE EYVVGPLPNP ARHEPYSNPA
     RRSPIPWTSR AIDPKEYALI MPIIENTTAR VYDILKESYG YTYRNCSARC LVALDSVPKG
     YRSGKRRSWI SFRRAGVGGV TYFIGFMMQV THESADPNEW HVSRVFYNNQ YFDSVEQLIT
     GYADGSVEKD TPDADVQEDD ILYPTFIRRG KPQPASPSRG PTLTEPGGRR YAVRGRHVEY
     MGWSFDWRLT TTQAMQLYDV RMNGERIAYE LSSQDATSFY SGGNPAMLNN LFLDSYWDFA
     KSFELVRGID CPETATFFNT LQQRSTKEPR LIQNSVCVFE LNAGIPLRRH FDSDFAGGFN
     FYGGMADHVL VLRHINTVDN YDYVYDYIFH QNGVIEVRVG LTGYILTSQD RTPYGYPLYG
     GIIGNVHQHS FNYKVDLDIL GTQNRFETVE ILLENITNPV RPELRHIQTR IQRNLRTTEK
     EAAVQYDFNR PKYYNFYSEE QKNRFGVNRG YRVQLNGIAK TLLPRQDWAA MRGVAWQDYQ
     LVVTQRKDSE PSSSSIYNQN DLYDPVVDFQ SFIDDDESIV DEDLVAWVTL STHHIPHSED
     FPTTATAGTQ MQFFLRPFNY YDEDPSVGSS NAVL
//
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