UniProt: K8EHE4

Database: UniProt
Entry: K8EHE4_9CHLO

LinkDB:  K8EHE4_9CHLO 
Original site:  K8EHE4_9CHLO

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Ontology (6)   
   GO (6)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
All databases (18)   

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ID   K8EHE4_9CHLO            Unreviewed;       686 AA.
AC   K8EHE4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=Bathy06g03420 {ECO:0000313|EMBL:CCO17426.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO17426.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO17426.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO17426.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FO082273; CCO17426.1; -; Genomic_DNA.
DR   RefSeq; XP_007512826.1; XM_007512764.1.
DR   AlphaFoldDB; K8EHE4; -.
DR   STRING; 41875.K8EHE4; -.
DR   GeneID; 19015323; -.
DR   KEGG; bpg:Bathy06g03420; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000198341; Chromosome_6.
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; 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:UP000198341};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          122..234
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          263..669
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        336
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        420
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         420
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   686 AA;  77014 MW;  ADDDA6FD5D5D3D02 CRC64;
     MSPGVTAHAL DELSSEEISQ LARVVRDNFS NSIRTTGKGV TNSSLKEEEG DPEKMMLFNY
     ITLAEPTREE LSANCGDGDA VHERRGEVMI IVPWTGEAYK YVIAVKSLEV VKVERVKKGQ
     QPLITPDDCL EAERICKNDE KVKAMMKERY GIEDLTMLVC DPWSVHVTEP GMEPLDWRKD
     DGEIPARLVQ TFLYWRDDDL DDNQYAHPID LLPVVDLNAG KVVDITCQDV PREIPMKSVN
     YHREKLKSNS YLANVWRDAM KPLEIVQPEG AAFEVDGRLV KWDKWTLRVG FNYREGLVLH
     DVKYDNRPIL HRASLVEMAV PYADPNPPYT RKCAFDVGDY GLGYCTDSLE LGCDCLGNIH
     YFDATLANSK GEPYVIKKAV CMHEEDHGLL WKHVEYRTGH SEARRSRRLV LSFIATVVNY
     EYLFYYYFQQ DGTIEFEIKL TGELSTNAIS AGESNDDPTH GVLVAPGVNS QIHQHMFCAR
     LDVAIDGNEN EVSEIDICSD TSTGSCQNVF GPVTTPLVTE LQARRVCDST KARVWKISNP
     SSLNPVTKKP VSYKLIPFTR GPAMPTLLTG PECAVTKKGE FATKNLWVTP YNWPNERWPA
     GEFTVQGALG EGLPEWTKDD RDISSGELVI WHAFGVVHIP RPEDFPVMPV EHTGFSLKPD
     GFFAGNPTID LPPPKSGKST CCSTKL
//

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