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Database: UniProt
Entry: C5DGP5_LACTC
LinkDB: C5DGP5_LACTC
Original site: C5DGP5_LACTC 
ID   C5DGP5_LACTC            Unreviewed;       684 AA.
AC   C5DGP5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   OrderedLocusNames=KLTH0D06996g {ECO:0000313|EMBL:CAR22587.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR22587.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR22587.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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; CU928168; CAR22587.1; -; Genomic_DNA.
DR   RefSeq; XP_002553025.1; XM_002552979.1.
DR   AlphaFoldDB; C5DGP5; -.
DR   STRING; 559295.C5DGP5; -.
DR   GeneID; 8295256; -.
DR   KEGG; lth:KLTH0D06996g; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   HOGENOM; CLU_011500_3_1_1; -.
DR   InParanoid; C5DGP5; -.
DR   OMA; VRNDPWI; -.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000002036; 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   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          246..643
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        401
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         401
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   684 AA;  76669 MW;  1A5A5367603808E4 CRC64;
     MHIFDPISDA EIRTTARLLK DLNGDAKVHF VQIDRLDPPK KQALRYLSVE RHGGAPLPRI
     PRRTYAYYYL NDRMPLYKAL CNVSDGRVIA NQATPEGTVG PLLPEDVEAV EAAILAHPAV
     QAEIAKLKLD ALSYNHSALG PLGYSVVCEP WMYGTDSPHD KIPLIQAYMY LKLDHPEANH
     YSIPLKFSPV FEYLTHAFVR IDYLPSGADE SLVHNTLPHT VLPTVEYHPE LLEDVPPRDG
     LKPLIVSQPE GASFTVDGSK ITWQDWEFRV ATNVREGLAI YDVHFKGRSL FYRASLEEMT
     VPYGDSRAPF HRKQAFDLGD CGFGNSANSL ALGCHCLGVI KYLDTRRSDS EGNPVLIPST
     VCMHEQDYGI LYLHKNYRNG KTVTTRRREF VVQTIATVAN YEYILNFVFD QAGAITVQVR
     ATGILSTMPN DDNNVTDFGT IVGPGVTAAY HQHLLSFRFD TRIDGDKNTV VYDDYVPMEE
     NTAMNPYNVG FRQVRSYMDK SGYIDQSPFT NRTYKVINEN SINPVTMKPV GYKFEMPAKQ
     MILASKNSYN VKRAHYATKQ FWVSKYHDDQ LYAAGEFTNQ SQGDTGLSKW ADGTESVRNT
     DTVVWATLAL THPPVTEQFP VMTSDFMQFL VTPASFFTKN PALDVPLANN NFNKSVYYED
     AQKAAGLATG ESQSSSASCC KSNI
//
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