ID   AMO1_ARTS1              Reviewed;         648 AA.
AC   Q07121;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Primary amine oxidase;
DE            EC=1.4.3.21;
DE   AltName: Full=Copper amine oxidase;
DE   AltName: Full=MAOXI;
DE   Flags: Precursor;
GN   Name=maoI;
OS   Arthrobacter sp. (strain P1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=47915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-54;
RP   358-381 AND 456-466.
RX   MEDLINE=93374858; PubMed=8366046;
RA   Zhang X., Fuller J.H., McIntire W.S.;
RT   "Cloning, sequencing, expression, and regulation of the structural
RT   gene for the copper/topa quinone-containing methylamine oxidase from
RT   Arthrobacter strain P1, a Gram-positive facultative methylotroph.";
RL   J. Bacteriol. 175:5617-5627(1993).
CC   -!- FUNCTION: The exact function of maoXI is not known.
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 subunit.
CC   -!- COFACTOR: Contains 1 topaquinone per subunit (By similarity).
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; L12983; AAA22076.1; -; Genomic_DNA.
DR   HSSP; P46881; 1IVW.
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; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; TPQ.
FT   PROPEP        1      9
FT                                /FTId=PRO_0000035675.
FT   CHAIN        10    648       Primary amine oxidase.
FT                                /FTId=PRO_0000035676.
FT   ACT_SITE    301    301       Proton acceptor (By similarity).
FT   ACT_SITE    385    385       Schiff-base intermediate with substrate;
FT                                via topaquinone (By similarity).
FT   METAL       436    436       Copper (By similarity).
FT   METAL       438    438       Copper (By similarity).
FT   METAL       595    595       Copper (By similarity).
FT   MOD_RES     385    385       2',4',5'-topaquinone (By similarity).
SQ   SEQUENCE   648 AA;  72761 MW;  B2F9E267492253B5 CRC64;
     MTLNAESEAL VGVSHPLDPL SRVEIARAVA ILKEGPAAAE SFRFISVELR EPSKDDLRAG
     VAVAREADAV LVDRAQARSF EAVVDLEAGT VDSWKLLAEN IQPPFMLDEF AECEDACRKD
     PEVIAALAKR GLTNLDLVCF EPWSVGYFGE DNEGRRLMRA LVFVRDEADD SPYAHPIENF
     IVFYDLNAGK VVRLEDDQAI PVPSARGNYL PKYVGEARTD LKPLNITQPE GASFTVTGNH
     VTWADWSFRV GFTPREGLVL HQLKFKDQGV DRPVINRASL SEMVVPYGDT APVQAKKNAF
     DSGEYNIGNM ANSLTLGCDC LGEIKYFDGH SVDSHGNPWT IENAICMHEE DDSILWKHFD
     FREGTAETRR SRKLVISFIA TVANYEYAFY WHLFLDGSIE FLVKATGILS TAGQLPGEKN
     PYGQSLNNDG LYAPIHQHMF NVRMDFELDG VKNAVYEVDM EYPEHNPTGT AFMAVDRLLE
     TEQKAIRKTN EAKHRFWKIA NHESKNLVNE PVAYRLIPTN GIQLAARDDA YVSKRAQFAR
     NNLWVTAYDR TERFAAGEYP NQATGADDGL HIWTQKDRNI VDTDLVVWYT FGMHHVVRLE
     DWPVMPRQNI GFMLEPHGFF NQNPTLNLPT STSTTQTGEA DTCCHNGK
//