ID AMO1_ASPNG STANDARD; PRT; 671 AA. AC Q12556; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Copper amine oxidase 1 (EC 1.4.3.6). GN Name=AO-I; OS Aspergillus niger. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 1-35; 538-565; 570-597 RP AND 635-654. RC STRAIN=AKU 3302 / M-62; RX MEDLINE=96203933; PubMed=8620882; 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: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + CC H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per dimer and 1 topaquinone per CC subunit. 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. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31869; AAB03385.2; -. DR HSSP; P12807; 1A2V. DR InterPro; IPR000269; CuNH_oxidase. DR Pfam; PF01179; Cu_amine_oxid; 1. DR Pfam; PF02727; Cu_amine_oxidN2; 1. DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1. DR PROSITE; PS01165; COPPER_AMINE_OXID_2; FALSE_NEG. KW Copper; Direct protein sequencing; Oxidoreductase; TPQ. FT DOMAIN 3 106 N2. FT DOMAIN 107 211 N3. FT MOD_RES 405 405 2',4',5'-topaquinone (By similarity). FT METAL 617 617 Copper (Potential). 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 //