ID A0A0A2LM97_PENIT Unreviewed; 679 AA.
AC A0A0A2LM97;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=PITC_037930 {ECO:0000313|EMBL:KGO77485.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77485.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77485.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77485.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO77485.1}.
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DR EMBL; JQGA01000150; KGO77485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LM97; -.
DR STRING; 40296.A0A0A2LM97; -.
DR HOGENOM; CLU_011500_3_1_1; -.
DR OMA; VRNDPWI; -.
DR OrthoDB; 34972at2759; -.
DR PhylomeDB; A0A0A2LM97; -.
DR Proteomes; UP000030104; 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 PANTHER; PTHR10638:SF60; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 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 Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 240..638
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 395
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 395
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 679 AA; 77055 MW; C9001DCDF34F56F4 CRC64;
MVTNQGLHPF DPITPEEIKL AVRILEATFP GVSLRYKRID VNEPIKKDVI AYIEAERLRR
PLPPPPARLL YVLFHRLDTG AFYKAILNAD KRTIVYAKEL PKEVQGPIDI DEVAGIEAMC
MKHPAVLAEI EKLQLPAGIT VCNDPWMYGT DSDNEDRRLF QCFMYLVEVD HPQNNHYSLP
CKFSPVFDAI THELIRMDYL PGGAGFETTP TQPWKPVKTV QYAHDLLGEP LRNDLKPYIV
QQPEGPSFSV IGNSVYWQKW RFRVGFNARE GLIIYNVTYD NRNIFYRLAV SEMTVPYGDP
RAPYHRKQAF DVGDTGFGMN ANQLALGCDC LGHIKYFDGY LNDSKGNPVE MKNVICMHEQ
DNGLQHKHTN YRSGAATVVR NRQLVLQMIC TVANYEYIFN YIFDQAANVE LEVRATGILS
TVPFDNENGE TVPWGTNVGA GVMAPFHQHM FSLRIDPAID GFKNTIYYED SVPMPEDEKN
PYLVGYTSES TVIRTAGTAN TSVDRHRVFK IRNDNVTNPI TYKPVAYKLM AAPSQMLLVS
KNAHGFRRAE FATKPIWVTK YQDDELYAAG EFTNQSRRAE GVETWVQRKD NVENEDVVLW
HTFGLTHNPR IEDFPVMPME RISIMLKPDG FFNKNPALDV PQSSQLFNKS SLHPEEQVAA
CCAGASSAGS KAKLYKRVD
//
