ID A0A1G4JH34_9SACH Unreviewed; 707 AA.
AC A0A1G4JH34;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=LANO_0D05006G {ECO:0000313|EMBL:SCU89460.1};
OS Lachancea nothofagi CBS 11611.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU89460.1};
RN [1] {ECO:0000313|EMBL:SCU89460.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT598448; SCU89460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4JH34; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000189911; Chromosome d.
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 PANTHER; PTHR10638:SF33; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
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 270..667
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 425
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 425
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 707 AA; 80492 MW; DF299B53582A70DD CRC64;
MPYFAIQISS TLPFVAVQHP APMTLHIFDP LQDCEIRTTA KLLKDFNGDA KVHFIQIDRL
DPPKKQAIKY LNIERHGGGK LPYIPRRTYA YYYLNDRMPL YKALCNVSDK RVIANQATPE
GTVGPLLPED ITAVEEAIMK HPKVLAEISK LKIDNLYYDH SRLGKLGYSV VCEPWMYGTD
SPNEKIPLIQ AYMYMKLDHP EANHYSIPLR FSPVFEYLTH KLVRIDFLPA GADEKYVKET
LPYRQFETVE YHPELIENTP TRKNLKPLIV SQPEGASFEI EGSKVKWQDW EFRISTNVRE
GFALYDVFFK GRSLFYRVAL NEMTVPYADP RAPFHRKQAF DLGDCGFGNT ANSLALGCHC
LGVIKYLDTR RADQEGNPVL IPSTICMHEQ DYGLLYLHKN YRNDNTVATR RREFVIQTIA
TVANYEYVVN LIFDQAGAIT VQVRATGILS TMPNDENMVT DFATIVGPGV TAPFHQHLLS
FRFDTRIDGD DNTVVYDDYV PMEENTAMNP YNVGFRQERT FMEKSGYVEQ SPFTNRTYKV
INEKSINPVT LKPVGYKFEM PAKQMIIASK NSYNAKRAHY ATQQFWVSKY HDDQLYAAGE
FTNQSQVDTG LCKWADGSES VRNTDTVVWA TLALTHPPAT EQFPVMTSDF LQFLVTPVSF
FTKNPALDVP LANNNFNKSV YYEDAQKSAG LASKDSSSTA SCCKSNI
//
