ID W6ZHT2_COCMI Unreviewed; 688 AA.
AC W6ZHT2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=COCMIDRAFT_1598 {ECO:0000313|EMBL:EUC49550.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC49550.1};
RN [1] {ECO:0000313|EMBL:EUC49550.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC49550.1};
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 -!- 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; KI963930; EUC49550.1; -; Genomic_DNA.
DR RefSeq; XP_007683825.1; XM_007685635.1.
DR AlphaFoldDB; W6ZHT2; -.
DR STRING; 930090.W6ZHT2; -.
DR GeneID; 19119902; -.
DR KEGG; bor:COCMIDRAFT_1598; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_1_1; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000054032; 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; -; 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 InterPro; IPR015800; Cu_amine_oxidase_N2.
DR PANTHER; PTHR10638:SF33; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 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 TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 13..101
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 244..646
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 656..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 405
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 405
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 688 AA; 76684 MW; 1FABA974203CAA18 CRC64;
MSGEQATTTA PWHPLAPLTA AELQKAAGII KASWPAHTDL HFKVVTLEEP PKTEVLKYLE
AEHGGKPLPS IPRKAFVNYY IRNTSKFHEA IVDLTSGRIE RNLLLGPFIH ANGDGDEIIA
IEKVALADEK VQAEIAKLEL PEGTVVISDP WIYGSDGIGD EDRLYQCFLY LRDPMNSSEA
DSNHYAMPLP ISPVVSTETM TVIRVDLLPT GVDKTIKPVG KYKIQPPNEY IPEAQKLRTD
LKPLNVVQPE GASFQVQQQG TSSVISWQKW QFRVGFNQRE GMVLYDVRYD NRSLFYRLSL
SDMNIPYADP RHPYHKKSAF DLGDAGAGIM ANNLKLGCDC LGSIYYLSSV LSDDKGGVID
MPNVVCIHEQ DAGIGFKHTN YRTGRAVVAR SRELVLQSII TVSNYEYILA FIFNQAGEIS
YEIRATGILS TQPIDEGVEV PFGTVVHPGV LAVHHQHIFS LRVDPMIDGY DNRLVYDEAF
PMPRSDFNPH GTGYYVQETV VEKSGGYDIA YENNRTFKIQ NPNVRNPVNG KAVAYKIQAP
PFQKILSDKD SFNYKRAEFS DHNIYVVKHK DGELYAGGTY TNQSRGGTGV RSWAERNDNV
KDTDLVVYIQ AGINHVPRIE DFPVMPCEIL KIHLKPVNFF DKNPALDVPP SEQAFNKSSL
LSEQHQQPSV TATVGKDGQC CAPQSAKL
//
