ID   AMOH1_SCHPO             Reviewed;         794 AA.
AC   O42890;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Putative primary amine oxidase 1;
DE            EC=1.4.3.21;
DE   AltName: Full=Copper amine oxidase 1;
GN   ORFNames=SPBC1289.16c, SPBC8E4.06;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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 (By similarity).
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; CU329671; CAB38696.1; -; Genomic_DNA.
DR   PIR; T39367; T39367.
DR   PIR; T50376; T39171.
DR   RefSeq; NP_596841.2; -.
DR   HSSP; P12807; 1A2V.
DR   GeneID; 2539624; -.
DR   KEGG; spo:SPBC1289.16c; -.
DR   GeneDB_Spombe; SPBC1289.16c; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004821-MON; -.
DR   BRENDA; 1.4.3.6; 653.
DR   ArrayExpress; O42890; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
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   2: Evidence at transcript level;
KW   Complete proteome; Copper; Metal-binding; Oxidoreductase; TPQ.
FT   CHAIN         1    794       Putative primary amine oxidase 1.
FT                                /FTId=PRO_0000064107.
FT   ACT_SITE    309    309       Proton acceptor (By similarity).
FT   ACT_SITE    394    394       Schiff-base intermediate with substrate;
FT                                via topaquinone (By similarity).
FT   METAL       445    445       Copper (By similarity).
FT   METAL       447    447       Copper (By similarity).
FT   METAL       604    604       Copper (By similarity).
FT   MOD_RES     394    394       2',4',5'-topaquinone (By similarity).
SQ   SEQUENCE   794 AA;  90127 MW;  81E0E1CAD73F54F9 CRC64;
     MAEESKAAEY FDPLDPLSFN ELRYVVNLVR KSYPEKQISF DVVTLSEPHK EEYVHWRYSS
     AHEGIPDRRA YVIVLEKEVP GVFEGIVNLT TGKIEKWEHS VDTCPIITAD LLAITDEIVR
     NDANVIEQCK ICGVPESGLS NVYCDPWTIG YDERYGSGRR LQQALMYYKP GDSGHLRSIP
     LDFCPIIDVD QKKVIAIDIP KVRRPIPQDV NSDNNLKKLE QEMEAMKMLK PLRITQPEGV
     NFRIKGRYIE WQNFCFHIGF NYREGIVLSD VVFNEDGHLR PLFYRISLTE MAVPFGAKGH
     SHHRKHAYDL GEYGVGYRTN PLSFTCGCEG VIHYMDADFV NYRGEITTIK NAISIHEEDD
     GVLFKYSDLR DRNANISARS IKLVVSQVFT AANYEYLVYW IFRMDGVIEC EIRLTGILNT
     NAINEDEDLK GHGTQVYPKI SAENHEHLFC LRINPMLDGL RNSVATVDAL RDKNGTLVSK
     YIIPETVTEA ISNYDSSTGR TWDICNLNKL HPYSGKPVSY KLISRDTSPV LSQPGTTNSD
     CSGFAENNIY VTPYMDDQIF PTGDYAPQAS DDTPKGLSKW ISDDPNAQIK NTDIVVWHTF
     GMIHFPAPED FPIMPAESIH LFLQPRNFFK HNPALDTSSS VNSTSEATSP NTHHENLRDT
     SQKRESHSTP HDYEPHVSDK NDKSVEDKLH FVQKDESRPK EPVVDAAQKH EGRSETLAQP
     GQQNANQSEE KQGGQNGSNG GHHHHHHHHY ITGHVYGGYH KHSGSGGHLV DMMKNISDVT
     HDFAMGNFRY HKYD
//