ID A0A0C4EBB2_MAGP6 Unreviewed; 642 AA.
AC A0A0C4EBB2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=MAPG_09959 {ECO:0000313|EMBL:KLU91439.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_09959T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU91439.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU91439.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU91439.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU91439.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_09959T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_09959T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_09959T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_09959T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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; ADBL01002557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876977; KLU91439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4EBB2; -.
DR STRING; 644358.A0A0C4EBB2; -.
DR EnsemblFungi; MAPG_09959T0; MAPG_09959T0; MAPG_09959.
DR VEuPathDB; FungiDB:MAPG_09959; -.
DR eggNOG; KOG1186; Eukaryota.
DR OMA; INWATHP; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000011715; Unassembled WGS sequence.
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; -; 1.
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:SF20; 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; 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:UP000011715};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..642
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010907131"
FT DOMAIN 212..600
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 351
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 351
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 642 AA; 72719 MW; 2B723187F58141A6 CRC64;
MKFLLALASL ATGLASTAAS ELVAENVRAE KRAVNSTYIP VKAPRDNLWS KITDQEQRDI
LSFIGREQNK SIPAELNFDQ STIWQLAPNK TEASLYLSGQ GAKPKRYARI LGDGDCVTRE
YMIGPLPVNN ETRAVSLDYL YRGNATLVSK SKWCDPNWGN ATLRRQAADE ARKISVVYKR
ALERRENKSP YEEKLLWDGN KLPHDDKEPP VSIAPGGARY EYDPEQNYVS WMDFSFFVAT
GPAGVSVHDI RYKGERVVYE LGMQEALAHY AGPDRVQTYA SYIDVTVGFT TYNMIPGYDC
PSYATYTDAF CLFEYTKDFP LSRHYVKEQN TYHAAKNTAF LLRTVNTVGN YDYMITYEFR
LDGSIEILVR ASGYIQGSTS VDEKDIWDYG FHIRKGLSGS MHDHVLNFKA DLDILGTKNS
LFKTQFVPHS QVFPWSNGSV VNTMKANRSF VTNEDQGRIN WAANSAATYA VVNRDKLNEN
GEFPGYKIHP TTGSSIHVTV QNSTVFPREI NWATHPLYAV RRKDTEPVSA HPVAVWDKGK
PPFVDFDSFF DGESPEQEDL VIYFNLGMHH MPDMYDLPVT TFLDAQSGMT LRPQNYLPSN
GWLSTRQQIH IENRKVDTYG REDLKGSYDL ANTKPPFYPG LI
//