ID Q6BQS6_DEBHA Unreviewed; 662 AA.
AC Q6BQS6;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN OrderedLocusNames=DEHA2E02640g {ECO:0000313|EMBL:CAG87660.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG87660.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG87660.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382137; CAG87660.1; -; Genomic_DNA.
DR RefSeq; XP_459444.1; XM_459444.1.
DR AlphaFoldDB; Q6BQS6; -.
DR STRING; 284592.Q6BQS6; -.
DR GeneID; 2902804; -.
DR KEGG; dha:DEHA2E02640g; -.
DR VEuPathDB; FungiDB:DEHA2E02640g; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_1_1; -.
DR InParanoid; Q6BQS6; -.
DR OMA; VRNDPWI; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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 PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
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:UP000000599};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 237..633
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 308
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 392
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 392
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 662 AA; 75018 MW; 11ACA088887CDD7B CRC64;
MTSIHPFDSV KDFEIRLASK LVKDAYPASA NVHFVQIDRV DPPKKDMIKY LDAEKLGETP
QAIPRVLYTY YYTNTLTFNK ALVNVTAGHI ITKTQLPHGT VGPYLPDDMM EWEKLCTNHP
LVKAEIEKLK LPPGYTVRND PWIYATDDPN ERRPLVQFFM YVLAGNGHTE SNHYSLPLKF
SPVFEAFTNK FIRIDYLPGG FDETITPTMP WKEVPCVEYH PDLNNEVNMR DVKPLLISQP
EGPSFSVNGS KVKWQGWEFR VATSAREGFA IYDASFKGRQ AFYRISLSEM TVPYGDPRAP
YHRKQAFDLG DCGFGVNGNH LSLGCDCLGV IKYMDGVGIH ANGEPFVVPN TVCMHEQDNG
LLYKHVNYRT NNAVVARRRE FIVQTIATVA NYEYIINVKF ITDGSINIET RATGILSTMP
IDENVKVPWG TIVGHNVMAA YHQHILSFRI DPSIDGHKNS VVYDDVVKLP KDKLNPYGVG
FITERKFVDR SGHIDQSPFT NRSYKIINEN KINPISKTPV GYKVVMPARQ MILADDDSFN
VKRAKFATEQ VWVTKYRDHE LFAAGEFTNQ SQRDEGLGTW ANGVDPVRNE DLVVWATVGF
THIPRVEDFP VMPVEIHNIE LVPFNFYDKN PALDIPQANN TFNKSVLSDS NTAEKACCKT
KI
//
