ID A0A2V3J6I3_9FLOR Unreviewed; 678 AA.
AC A0A2V3J6I3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=BWQ96_00394 {ECO:0000313|EMBL:PXF49742.1};
OS Gracilariopsis chorda.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilariopsis.
OX NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF49742.1, ECO:0000313|Proteomes:UP000247409};
RN [1] {ECO:0000313|EMBL:PXF49742.1, ECO:0000313|Proteomes:UP000247409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF49742.1,
RC ECO:0000313|Proteomes:UP000247409};
RC TISSUE=Whole body {ECO:0000313|EMBL:PXF49742.1};
RX PubMed=29688518; DOI=10.1093/molbev/msy081;
RA Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT provides insights into genome size evolution in Rhodophyta.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PXF49742.1}.
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DR EMBL; NBIV01000002; PXF49742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3J6I3; -.
DR STRING; 448386.A0A2V3J6I3; -.
DR Proteomes; UP000247409; Unassembled WGS sequence.
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; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
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:UP000247409};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 123..221
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 261..662
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 418
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 418
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 678 AA; 75451 MW; 932FC5CA5D8B9205 CRC64;
MVAHASQYVV SGEDSSSTLN DQQPFLSMAP AAESSPSTRE TSPCHPLPLS PLSATEIREA
ARLSREYLSD NARFSVITLD EVCQNRAAIV IALLPPDATA HKLHVNLVTS EIRQLPVPEG
AQPVLTPDDC HLAEKIVKAD SRVRELISKR YGIDDIDSLV CDPWSVHVSG NYAPLSFRED
NQAARLVQTF LYRRDHPVDN HYAHPIDILP VVDLNMRTVV TVEGIERAPP TLSSTAVNYH
PDLLEKNEYL PTQTRTTLRP IQVVQPKGPS FTVNGYNVEW EKWSFTIGFN YREGLVLHNV
CHDSRSVVKR ASLVEMAVPY ADPHPPFERK CAFDVGDYGL GYCANSLELG CDCLGAIHYF
DAVLPDSRGE PYVIRKAVCM HEEDVGLLHK HVEYRTGHSE SRRARRLVVS FIATVVNYEY
LFYWYLHHDG SISHEIKLSG ELSTNLLSEG ETHPTAGVIV APGVNAQIHQ HMFCARLEMA
VDGAQNSVEE VNLVAAEEGS HNPFGNIFRV ESTLLRSEQD AQRDAAAART WRIFNPHKSN
TISGKKVAYK LVPYTFGAFQ PPLLTTDDSA VSKRGRFAKK AIWVTPYRKD EQFPAGEFPT
QSLGGDGLPS WTSQNRSIVD ERIVIWHSFG VAHVPRTEDF PIMPCESTGF TLKPDCFLMG
NPGVDIPRSV EKSSVCCS
//
