ID M2SYZ0_COCSN Unreviewed; 1055 AA.
AC M2SYZ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Amine oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCSADRAFT_197311 {ECO:0000313|EMBL:EMD67530.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD67530.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD67530.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|ARBA:ARBA00007983}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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DR EMBL; KB445639; EMD67530.1; -; Genomic_DNA.
DR RefSeq; XP_007697165.1; XM_007698975.1.
DR AlphaFoldDB; M2SYZ0; -.
DR STRING; 665912.M2SYZ0; -.
DR GeneID; 19134010; -.
DR KEGG; bsc:COCSADRAFT_197311; -.
DR eggNOG; KOG0764; Eukaryota.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_010620_0_0_1; -.
DR OMA; VHVGFNY; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000016934; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
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:InterPro.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier 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; IPR015802; Cu_amine_oxidase_N3.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF86; COPPER AMINE OXIDASE 1-RELATED; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 21..104
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 111..212
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 238..650
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REPEAT 756..844
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 855..942
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 957..1039
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 399
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 399
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 1055 AA; 118057 MW; 4B4E7BAB7E970CB1 CRC64;
MSLDRLKQAA SHITGIGAPP HPFDPLSEPE IEQAVAIIRK EHKDVFFNAI TLWEPRKAEM
MKWLKDPDHT PRPHRVADVV CIGRGSKVFD GQVDLTEGKI VSWALTDDVQ PLITMEDLQI
VETVVRKDPK VIEQCGIIGI PPEDMHKVYC DPWTIGYDER FGTKVRLQQA LMYYRPHPDD
SQYTYPLDFC PIYNSDTQEI IHIDVPPVRR PLNRAPPNNY HASAIEAEGG FKTDLKPINI
TQPEGVSFKM DGRYISWANW KLHIGFNYRE GIVLSNITFN DKGTVRDTFW RLSLAEMVVP
YGNPEHPHQR KHAFDLGEYG GGYMTNSLSL GCDCKGAIHY MDAAFVNRAG QSTTIKNAIC
IHEEDAGILF KHTDFRDDSV TVTRARKLII SHIFTAANYE YCVYWIFHLD GTIQLEIKLT
GILNTYAMLP GEDLKGWGTE VYPGVNAHNH QHLFCMRIDP NIDGPENTVF MVDAARGDGE
VGSAENKYGN AFYAKKTKLS TPEQAATGYN GATSRTWEIA NTNKLNPYSK KPVSYKLVSR
EVPELLPKPG SLVWKRAGFA RHAVHVTKYD DSQIHPAGRH VPQTSGEPSQ GIPAWIEANP
NENLDNTDVV LWHTFGITHF PSPEDFPIMP AEPMTLLLRP RNFFTRNPCL DIPPSYCSVP
SGVRQGNTLV DKLSRMAFGE EKTEAPPATC CSDQKFGVAF ILHSTYPAPS ASPPVPEDVL
GEIANPSLKP AMPRAFPPVK QDVHSKQSSA PQSALSASVI ESIAGFSAGV VSCLAAHPLD
LLKNRLQLNT TSRSRPGDSF RILRNVIRDE GGVRALYRGL WPNLLGNSLG WGLYFLFYGN
LKELFQSRRQ KGEHLGSAEF FSASIIAGLL TGACTNPIWV VKTRMLERGA NHPSAYKSMA
VGLRHVYETR GLKGLWAGFL PSSLGVLHGA VQFSIYENMK KRRALHIGGQ DKLSNWEYVY
MSGGSKLLAG AITYPYQPIR ARLQQYNAAQ QYNGLLDVLR KTYQNEGFLA FYKGVIPNTL
RVIPTTVVTF LVYENTKLYL PKVFADDEQQ FHEED
//
