ID A0A2Y9PHY7_DELLE Unreviewed; 755 AA.
AC A0A2Y9PHY7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=AOC1 {ECO:0000313|RefSeq:XP_022444881.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022444881.1};
RN [1] {ECO:0000313|RefSeq:XP_022444881.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022444881.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_022444881.1; XM_022589173.1.
DR AlphaFoldDB; A0A2Y9PHY7; -.
DR STRING; 9749.A0A2Y9PHY7; -.
DR KEGG; dle:111182632; -.
DR InParanoid; A0A2Y9PHY7; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
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 InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638:SF3; AMILORIDE-SENSITIVE AMINE OXIDASE [COPPER-CONTAINING]; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 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 Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..755
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016106252"
FT DOMAIN 44..130
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 146..246
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 304..711
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 464
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 464
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 755 AA; 85901 MW; 0C509AA2DC1369B1 CRC64;
MGRKTLALGW AGAAILVLQT LAAAEGSPRT PGNKGRVFAD LSAQELKAVH SFLWSQKELR
LQPSSTLTMA KNSVFLIEML LPKKQHVLKF LDKGHRAPVR EARAVIFFGA QEHPNITEFA
VGPLPRPHYM RHLPHKPRHQ ASWASRPMCK AEYTLLSHTL EEASKPLHQF FRRTTGFTFG
NCHERCLTFT DVAPRGLASG QRRSWFILQR HMEGYFLHPT GLELLVDHAS TNPQDWTVEQ
VWYNGKFYRS PAELAQKYDD GEVDAVVLED PLAKDKDGEN LPEAALFSFY QPRGDFAITK
NGPRLVQPEG PRYSLEGNTV LYGGWSFAFR LRSSSGLQVL DVHFGGERIA YEVSVQEAVA
LYGGHTPAGM QTKYIDVGWG LGSVTHELAP GIDCPETATF LDALHYYDAD GPVLYPRALC
LFEMPTGVPI RRHFNSNFSD GFNFYAGLKG QVLVLRTTST VYNYDYIWDF IFYPNGVMEA
KMHATGYVHA TFYTPEGLRH GTRLHTHLIG NMHTHLVHYR VDLDVAGTKN SFQTLHVKLE
NSTNPWSPRH RLVQPTLQET RFSRERQAAF LFRQTLPKYL LFTSPKKNPW GHKRSYRLQI
HSMADQVLPP GWQEERAVTW ARYPLAVTKY RESELYSSSI YNQNDPWDPP VVFEEFLHNN
ENIEDEDLVA WVTVGFLHIP HSEDIPNTAT PGNSVGFLLR PFNFFPEDPS LASRDLVVVW
PLENGSTYVQ RWIPEEDGDC LMPPPFSYNG TYRPV
//
