ID   AMO_KLEAE      STANDARD;      PRT;   755 AA.
AC   P49250;
DT   01-FEB-1996 (Rel. 33, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Copper amine oxidase precursor (EC 1.4.3.6) (Monamine oxidase)
DE   (Tyramine oxidase).
GN   Name=maoA; Synonyms=tynA;
OS   Klebsiella aerogenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=28451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 31-41.
RC   STRAIN=W70;
RX   MEDLINE=92210491; PubMed=1556068;
RA   Sugino H., Sasaki M., Azakami H., Yamashita M., Murooka Y.;
RT   "A monoamine-regulated Klebsiella aerogenes operon containing the
RT   monoamine oxidase structural gene (maoA) and the maoC gene.";
RL   J. Bacteriol. 174:2485-2492(1992).
CC   -!- FUNCTION: Active on tyramine, tryptamine, beta-phenethylamine and
CC       dopamine.
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 and 1 topaquinone per subunit.
CC   -!- SUBCELLULAR LOCATION: Periplasmic.
CC   -!- INDUCTION: By tyramine and catecholamines.
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 as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; D10208; BAA01060.1; -.
DR   HSSP; P46883; 1OAC.
DR   InterPro; IPR000269; CuNH_oxidase.
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.
KW   Catecholamine metabolism; Copper; Direct protein sequencing;
KW   Metal-binding; Oxidoreductase; Periplasmic; Signal; TPQ.
FT   SIGNAL        1     30
FT   CHAIN        31    755       Copper amine oxidase.
FT   ACT_SITE    413    413       Catalytic base (By similarity).
FT   MOD_RES     496    496       2',4',5'-topaquinone (By similarity).
FT   METAL       554    554       Copper (Potential).
FT   METAL       556    556       Copper (Potential).
FT   METAL       719    719       Copper (Potential).
SQ   SEQUENCE   755 AA;  83577 MW;  7B5552283CD93EFF CRC64;
     MANGLKFSPR KTALALAVAV VCAWQSPVFA HGSEAHMVPL DKTLQEFGAD VQWDDYAQMF
     TLIKDGAYVK VKPGAKTAIV NGKSLDLPVP VVMKEGKAWV SDTFINDVFQ SGLDQTFQVE
     KRPHPLNSLS AAEISKAVTI VKAAPEFQPN TRFTEISLHE PDKAAVWAFA LQGTPVDAPR
     TADVVMLDGK HVIEAVVDLQ NKKILSWTPI KGAHGMVLLD DFVSVQNIIN TSSEFAEVLK
     KHGITDPGKV VTTPLTVGFF DGKDGLQQDA RLLKVVSYLD TGDGNYWAHP IENLVAVVDL
     EAKKIIKIEE GPVIPVPMEP RPYDGRDRNA PAVKPLEITE PEGKNYTITG DTIHWQNWDF
     HLRLNSRVGP ILSTVTYNDN GTKRQVMYEG SLGGMIVPYG DPDVGWYFKA YLDSGDYGMG
     TLTSPIVRGK DAPSNAVLLD ETIADYTGKP TTIPGAVAIF ERYAGPEYKH LEMGKPNVST
     ERRELVVRWI STVGNYDYIF DWVFHDNGTI GIDAGATGIE AVKGVLAKTM HDPSAKEDTR
     YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NTLVAMDPEV KPNTAGGPRT STMQVNQYTI
     DSEQKAAQKF DPGTIRLLSN TSKENRMGNP VSYQIIPYAG GTHPAATGAK FAPDEWIYHR
     LSFMDKQLWV TRYHPTERYP EGKYPNRSAH DTGLGQYAKD DESLTNHDDV VWITTGTTHV
     ARAEEWPIMP TEWALALLKP WNFFDETPTL GEKKK
//