ID   AMO1_ASPNG              Reviewed;         671 AA.
AC   Q12556;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Copper amine oxidase 1;
DE            EC=1.4.3.22;
GN   Name=AO-I;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-35; 538-565;
RP   570-597 AND 635-654.
RC   STRAIN=AKU 3302 / M-62;
RX   MEDLINE=96203933; PubMed=8620882;
RX   DOI=10.1111/j.1432-1033.1996.0255n.x;
RA   Frebort I., Tamaki H., Ishida H., Pec P., Luhova L., Tsuno H.,
RA   Halata M., Asano Y., Kato Y., Matsushita K., Toyama H., Kumagai H.,
RA   Adachi O.;
RT   "Two distinct quinoprotein amine oxidases are induced by n-butylamine
RT   in the mycelia of Aspergillus niger AKU 3302. Purification,
RT   characterization, cDNA cloning and sequencing.";
RL   Eur. J. Biochem. 237:255-265(1996).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=AKU 3302 / M-62;
RA   Frebort I., Cernikova V., Hirota S., Yamada M., Adachi O., Pec P.;
RT   "Reassessment of the active site and the primary structure of the
RT   amine oxidase AO-I from Aspergillus niger AKU 3302.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Histamine + H(2)O + O(2) = (imidazol-4-
CC       yl)acetaldehyde + NH(3) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 copper ion per dimer.
CC   -!- COFACTOR: Contains 1 topaquinone per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- INDUCTION: By N-butylamine.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent
CC       autoxidation of a specific tyrosyl residue (By similarity).
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
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DR   EMBL; U31869; AAB03385.2; -; mRNA.
DR   PIR; S71320; S71320.
DR   HSSP; P12807; 1A2V.
DR   BRENDA; 1.4.3.6; 277.
DR   GO; GO:0008131; F:amine oxidase activity; IEA:EC.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:cellular amine metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR015800; Cu_amine_oxidase_N2.
DR   InterPro; IPR015801; Cu_amine_oxidase_N2/3.
DR   InterPro; IPR015802; Cu_amine_oxidase_N3.
DR   Gene3D; G3DSA:3.10.450.40; CuNH_oxidase; 2.
DR   Gene3D; G3DSA:2.70.98.20; Lyase_8_central; 1.
DR   PANTHER; PTHR10638; CuNH_oxidase; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   Pfam; PF02728; Cu_amine_oxidN3; 1.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; TPQ.
FT   CHAIN         1    671       Copper amine oxidase 1.
FT                                /FTId=PRO_0000064110.
FT   REGION        3    106       N2.
FT   REGION      107    211       N3.
FT   ACT_SITE    321    321       Proton acceptor (By similarity).
FT   ACT_SITE    405    405       Schiff-base intermediate with substrate;
FT                                via topaquinone (By similarity).
FT   METAL       455    455       Copper (By similarity).
FT   METAL       457    457       Copper (By similarity).
FT   METAL       617    617       Copper (By similarity).
FT   MOD_RES     405    405       2',4',5'-topaquinone (By similarity).
SQ   SEQUENCE   671 AA;  75303 MW;  7413DF262A1BAE82 CRC64;
     MLPHPLAILS EEETNIARNV ILAQHPNTVI DFREIYLSEP PKAQLLEFLA LEHSGRLSPT
     SPRPPRLALC QYDVIGNDRI PSFEESVVDV GTRQRVQHRV VGKEHHASLT LSEFDTLVER
     CFASPLFQKA LADFDLPEGF EVVIEPWPYG GLDYVEEKRR YFQGLCFATD KRKNNPDANF
     YSYPLPLIPV MDALTQEIIR VDRPATGGKG EGLTEQTFKR DIIGHCKDSD YVPELNPGGT
     RKDLKPLNVV QPEGPSFRIT EESLVEWQKW RFRVAFNPRE GATIHDVWYD GRSVLYRLSV
     SEMTVPYADP RPPFHRKQAF DFGDGGGGNM ANNLSIGCDC LGVIKYFDAV MTGADGSAKK
     MPNAICLHEQ DNGIGWKHSN WRTGRAVVTR HRELVVQFII TLANYEYIFA YKFDQSGGIT
     VESRATGILN VVNIDAGKVS EYGNVVSGGV LAQNHQHIFC VRIDPAIDGP NNSVQVEESH
     PVPMNAVTNP NGNFYKVNTE TMERAGFFDA APELNRTVKM VNPHKKNPIS QKPVGYKFIP
     LATQRLLADP NSIQARRAQF AQHHVWVTKY RDGELYAGGR YTLQSQEEIE GVSDAVKRGD
     SVVDTDVVVW STFGITHNPR VEDWPVMPVE IFQLMIRPAD FFTANPSLDV PSDKNISSRV
     VGNDCCRNAH I
//