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Database: UniProt
Entry: C4R8F6_KOMPG
LinkDB: C4R8F6_KOMPG
Original site: C4R8F6_KOMPG 
ID   C4R8F6_KOMPG            Unreviewed;       786 AA.
AC   C4R8F6;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   OrderedLocusNames=PAS_chr4_0621 {ECO:0000313|EMBL:CAY71881.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY71881.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY71881.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392322; CAY71881.1; -; Genomic_DNA.
DR   RefSeq; XP_002494060.1; XM_002494015.1.
DR   AlphaFoldDB; C4R8F6; -.
DR   SMR; C4R8F6; -.
DR   STRING; 644223.C4R8F6; -.
DR   EnsemblFungi; CAY71881; CAY71881; PAS_chr4_0621.
DR   GeneID; 8201330; -.
DR   KEGG; ppa:PAS_chr4_0621; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   HOGENOM; CLU_015739_0_0_1; -.
DR   InParanoid; C4R8F6; -.
DR   OMA; CMFEIDK; -.
DR   OrthoDB; 5490352at2759; -.
DR   Proteomes; UP000000314; Chromosome 4.
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; IPR015328; DUF1965.
DR   PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   Pfam; PF09248; DUF1965; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
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   Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..786
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009950949"
FT   DOMAIN          92..146
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          241..294
FT                   /note="DUF1965"
FT                   /evidence="ECO:0000259|Pfam:PF09248"
FT   DOMAIN          323..725
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        397
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        477
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         477
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   786 AA;  89651 MW;  7960AA05E7F98FA7 CRC64;
     MRLTNLLSLT SLVALAVAVP DFYQKREAVS SKEAALLRRE ATECVSNENV LVEAPKSNIW
     TSLSKDEVQE VLDLLHSTYN ITEVTKSDFF SNYVLWIETL KPNKTEALTY LDEDGDLPPR
     NARTVVYFGE GEEGYFEELK VGPLPVSDET TIEPLSYYNT NGKSKLPFDV GHLDRIKSAA
     KSAFLNENLN TTTMRTVLED LIGVPYEDMG CHSAAPQLHD PATGAVVDYG TCNINTENDA
     ENLVPTGFFF KFDMTGRDVS QWKMLEYIYN NKVYNSAEEL YEATKKDDFV RLPKIDIDNL
     DWTVIPRNDS APIRHLDDRK SPRLIEPEGR RWAYDADEEY FSWMDWGFYT SWSRDTGISF
     FDITFKGERI VYELSLQELI AEYGSDDPFN QHTFYSDISY GVGNRFSLVP GFDCPSTAGY
     FTTDTFEYDE FYNRTLSYCV FENQEDYSLL RHTGASYSAV TQNPTLNIRF ISTIGNYDYN
     FLYKFFLDGT LEVSVRAAGY IQAGYWNPET SAPYGLKIHD VLSGSFHDHV LNYKVDLDVG
     GTKNRATQYV MKDVDVEYPW APGKVYNTKQ IAREVFENED FNGINWPENG QGILLIESAE
     ETNSFGNPRA YNIMPGAGGV HRIVKNSRSG PETQNWARSN LFLTKHKDTE LRSSTALNTN
     ALYDPPVNFN AFLDNESLDG EDIVAWVNLG LHHLPNSNDL PNTIFSTAHA SFMLTPFNYF
     DSENSRDTTQ QVYYTYDDET EESSWEFYGN DWSSCGVEVA EPNFEEYVYG RGTRINKKMT
     NSDEVY
//
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