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Database: UniProt
Entry: I0Z270_COCSC
LinkDB: I0Z270_COCSC
Original site: I0Z270_COCSC 
ID   I0Z270_COCSC            Unreviewed;       703 AA.
AC   I0Z270;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=COCSUDRAFT_28332 {ECO:0000313|EMBL:EIE24739.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC   Coccomyxa subellipsoidea.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE24739.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE24739.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE24739.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA   Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA   Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58001; EC=1.4.3.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001138};
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:EIE24739.1}.
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DR   EMBL; AGSI01000005; EIE24739.1; -; Genomic_DNA.
DR   RefSeq; XP_005649283.1; XM_005649226.1.
DR   AlphaFoldDB; I0Z270; -.
DR   STRING; 574566.I0Z270; -.
DR   GeneID; 17042740; -.
DR   KEGG; csl:COCSUDRAFT_28332; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000007264; Unassembled WGS sequence.
DR   GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
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; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF94; PRIMARY 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   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:UP000007264};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          38..115
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          138..232
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          267..673
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          680..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        428
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         428
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   703 AA;  78104 MW;  1AE0B132FEFAE0B9 CRC64;
     MAPSTTVTKP TFVDNLLGLV SRPALTPHQI GAVPTTAHPL DPLTAAEVSA AGKACRLHAD
     SLGLTQLRFN AITLEEPPKA ALLEYEASGR RLAKPPRRAH CIVQLPSEPN SSVAEVLVDL
     SSPVPAVLNW VKVEGVQPMV TIEDCVEAEE IVKADPGIRG LLKDRYGITD MDMVAADPWY
     YGDRFAEESK YSDGRIIQCF MYVRSGSVHD NHYAHPLDLV VFLDMNTGRV LDTLMQATSP
     VIPQLSTNYL APLVQKERGF RSGLKPLNIV QPEGPSFQVH GNEVSWQKWN MRVSFNYREG
     LVLHNVGYED GGRVRPVLHR ASTVEIIVPY GDPRSPFHKK CAFDVVDYGL GFSCSSLELG
     CDCLGHIHYF DAMLNTNKGE PMLIKKAVCM HEEDHGLLWK HVEYRTGHSE VRRSRRLVLS
     FVATIANYEY GFFWYFYQDG TIEHEVKLTG CLSTNMLSEG EGPLPTHGTL LAPGLNAQIH
     QHFFCVRLDM AVDDPHGGRN LTVNCDSMPL GPDNPNGVGF TATETPFETE LQAVREVDPR
     RSRVWKIKNM HSRNSITGVP VAWKLMPFAS PPVYAHPSNE HSRRGAFATK QLWVTPYSDD
     EKFPAGDYPL LAGDTNSIAN WTSLDRKIKE SDCVVWHSFG VTHVPRLEDW PVMPVERVGF
     HLKPVNFFDA NPGMDIAPLP NKASREHQGS SAACESCGPQ SKL
//
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