(data stored in SCRATCH zone)

SWISSPROT: Q750M9_ASHGO

ID   Q750M9_ASHGO            Unreviewed;       677 AA.
AC   Q750M9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=AGOS_AGL073W {ECO:0000313|EMBL:AAS54417.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54417.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54417.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- COFACTOR:
CC       Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
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=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600269-51};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|PIRSR:PIRSR600269-51};
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|RuleBase:RU000672}.
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DR   EMBL; AE016820; AAS54417.2; -; Genomic_DNA.
DR   RefSeq; NP_986593.2; NM_211655.2.
DR   STRING; 33169.AAS54417; -.
DR   EnsemblFungi; AAS54417; AAS54417; AGOS_AGL073W.
DR   GeneID; 4622892; -.
DR   KEGG; ago:AGOS_AGL073W; -.
DR   HOGENOM; HOG000250947; -.
DR   InParanoid; Q750M9; -.
DR   KO; K00276; -.
DR   OMA; NNHYSLP; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR   Gene3D; 2.70.98.20; -; 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; PTHR10638; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   SUPFAM; SSF49998; SSF49998; 1.
DR   SUPFAM; SSF54416; SSF54416; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q750M9.
DR   SWISS-2DPAGE; Q750M9.
KW   Copper {ECO:0000256|RuleBase:RU000672};
KW   Metal-binding {ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   TPQ {ECO:0000256|PIRSR:PIRSR600269-50, ECO:0000256|RuleBase:RU000672}.
FT   DOMAIN          245..646
FT                   /note="Cu_amine_oxid"
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   677 AA;  75639 MW;  09370B203B73F697 CRC64;
     MPHIFDSVSD DEIRTTARVV KALHGDAKIQ FSQIDRLDPP KQLALEYLAA ERQGSALPEV
     PRRTYCYYYR NQTVPLRTAV VDVAVGAVLS DEAAPKGVVG PMCPEGMQAA ESAVLAHPVV
     QQEIALLGLD KLHYDHPRLG RLRYKVTCDT WMYGRDTPGA GPPLVQAYMY VQLDHPDANH
     YSMPLRFSPV FEYLTHKFVR IDYLPTGADA ATLQKTLPFK QVKSLEYHPN LLDDATPRAG
     LKPLQISQPS GVSFAVEGSR VTWQGWDFRV ATNVREGFAL YDVHFKGRSL FYRISLNEMT
     VPYGDGRPPF HRKQAFDLGD CGFGATAGSL GLGCHCVGVV KYLDTRRTDL DGNPVLVPSS
     VCMHEQDYGI LHLHRNFRNN SEVVTRRREF VVQCVATVAN YEYILNYVFD QAGAITVQVR
     ATGILSTVPV DDDVNTDFST IVGPGVTAPF HQHLLSFRFD TRLDGDENTV VYDDYVADAP
     GGDMNRYNVA FRQKRTVLDR SGYIEQSPFT NRAFKVINEK SINPVTRRPV AYKFDMPARQ
     MLIALPDSFN ARRAKYSTQQ FWVCRHADDR RYAAGEFTNQ SERDSGLSVW ADGSESVRNT
     DIVVWPTLAL THAPVTEQFP VMASDFMQFL VTPASFFTEN PALDIPMANN AFHGSAYYED
     NHAAAGQDAA ACCKGNL
//

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