ID A0A179F4K2_METCM Unreviewed; 731 AA.
AC A0A179F4K2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=VFPPC_10119 {ECO:0000313|EMBL:OAQ60039.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ60039.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ60039.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ60039.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:OAQ60039.1}.
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DR EMBL; LSBJ02000004; OAQ60039.1; -; Genomic_DNA.
DR RefSeq; XP_018138000.1; XM_018288549.1.
DR AlphaFoldDB; A0A179F4K2; -.
DR STRING; 1380566.A0A179F4K2; -.
DR GeneID; 28852543; -.
DR KEGG; pchm:VFPPC_10119; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000078397; Chromosome 4.
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; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY 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.
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:UP000078397};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 6..101
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 251..676
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 607..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 409
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 409
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 731 AA; 81201 MW; 1F3F67F0453AD3EC CRC64;
MATAPHPLTQ LSVDEFTKAR DIIVKLYGGS QSVYFRQINL EEPSKETLIP YLEAEHAGTL
TADTPRPARQ AHVEYDLIKA EKHEAVRAVV DLDAGKVVSS DTAAANRHPY FTTDEFTQFF
DHCLASDLFK DAMSEFELPE GFEITIDPWP YGPSDNEDDP RIMQGLVFAR DARKNHPDTN
HYGYPIPIIP VMDWVTKKII RVDRLATGGS EDGLEPAPRG DKPKKLFENA KSAEWVPELL
DQPVRTDLKP LNVVQPEGAS FSVQEDGLIE WQKWRFRLGF TPREGAVLHD VCYENRPVFY
RLSFSELTVP YGDPRPPFHR KQAFDFGDGG IGRMANNLTL GCDCLGAIHY VDGLLSAPDG
SPTPAKSVVC LHEQDNGILW KHTNFRTNNA IVARSREFVV QQLCTLANYE YLFQYKLDLA
GGITLETRAT GMVSVVAIDE GKTSKYGNVV SPGILAQNHQ HIFAARIDPA IDSYRDNQVV
VEESHGVKKN PKTNPHGNLY EVRRQVVDKA TYVDAEPRHN RTMKMENPKK QNAISGKNLA
YKIIAPATQM ILADEESVHT QRAQFAQHNA WVTGYRDGEF WVAGEFTNQS RFEEGGVGDM
VRRGDWFTEE GKPNGVNGSN GTNGSSDNHG QKSSPVVWPV YGFTHNPRVE DWPVMPMEMY
QIHLRPTDFF EANPALDVPS KKNEASVLVP CCGKNGVTNG NGCGSVQKDP VAHLQGSNNG
ADAKAAGANV A
//
