ID A0A0B4HDX9_METMF Unreviewed; 782 AA.
AC A0A0B4HDX9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
DE Flags: Fragment;
GN ORFNames=MAJ_06120 {ECO:0000313|EMBL:KID97840.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID97840.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KID97840.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID97840.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KID97840.1}.
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DR EMBL; AZNE01000029; KID97840.1; -; Genomic_DNA.
DR RefSeq; XP_014576834.1; XM_014721348.1.
DR AlphaFoldDB; A0A0B4HDX9; -.
DR HOGENOM; CLU_015739_0_0_1; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000031176; 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 InterPro; IPR015328; DUF1965.
DR PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 2.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF09248; DUF1965; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
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:UP000031176};
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..782
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002104084"
FT DOMAIN 90..151
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 239..307
FT /note="DUF1965"
FT /evidence="ECO:0000259|Pfam:PF09248"
FT DOMAIN 321..407
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT DOMAIN 408..692
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 445
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 445
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KID97840.1"
SQ SEQUENCE 782 AA; 87039 MW; 8C7E52A33FB5DB0B CRC64;
MVPTFFSSVL ALIDWLSSAA NPSSSSCKKW SASPTPVHMH HMHLCESRQP AVSAPHPNIW
GDLTDEEAAG VIDLLHRQST GLNLTTEDAA GSWDNKILLV ELLAPNKSDT LPFLTNKTTT
PPPRCARATL MFGATPNPYL QDYVVGPLPV ANNTQVQPLQ FLYNNAGKGK VAVDFADRSA
VDHYVKDVGM SVADITKRLW DGTLNDTLGL LPIFPPWKEN GSLVLWSGFV NNPTSTFDSE
TILPLGLYFG VDVMGRDPSK WSVIGWYYDG KYYPTTNAFR AAAASRNFTL LGANSDGPWA
QIGRQGNPMK FDHLPPPTAI MPGPNRFSVD AKENYVEWMD FSFFLSYYRD NGLRLFNVQY
KGRRILYELG LQEALALYAG NDPVLSGTTY FDSKPGVGPS VVSLVDGLFE FDQGYPIQRH
STANYTSVTK NIAFTVRSIS TIGNYDYMFS YNFFLDGSIE VSVRASGYIH GGFSANNEEY
GWKIHDNLSG SMHDHVLTYK ADIDVLGEKN SLQKVEFVPA TIEYPWSNGA KRNTMKLQKS
FVQNENEAKI NWAPNGAAMY AIVNKEAKNK FGEYPGYRFT PATSNVIFLT ISNSSNVMNA
VNFADHHFYV TKQKDTEAQG THPYNVLNPA DPLIDFAKFF DGESLDQEDL VLWFNLGMHH
APHTGDLPNT MFTTAHSALI IEPLNYLEMD ASRATSQQVR LNYKDGKVQS IKTFGSQNMT
CHVDASQLMP KLWRDKGTVS VLTFVPGQSL IHPILEPPRQ VTTMRTRKTP RVSSEYKVAN
VT
//
