ID   A0A399JFK5_9MICC        Unreviewed;       652 AA.
AC   A0A399JFK5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=DWB68_13435 {ECO:0000313|EMBL:RII41286.1};
OS   Galactobacter valiniphilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Galactobacter.
OX   NCBI_TaxID=2676122 {ECO:0000313|EMBL:RII41286.1, ECO:0000313|Proteomes:UP000265419};
RN   [1] {ECO:0000313|EMBL:RII41286.1, ECO:0000313|Proteomes:UP000265419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JZ R-35 {ECO:0000313|EMBL:RII41286.1,
RC   ECO:0000313|Proteomes:UP000265419};
RA   Hahne J., Isele D., Lipski A.;
RT   "Arthrobacter sp. nov., isolated from raw cow's milk with high bacterial
RT   count.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|RuleBase:RU000672};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC       ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RII41286.1}.
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DR   EMBL; QQXK01000031; RII41286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399JFK5; -.
DR   Proteomes; UP000265419; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   InterPro; IPR015802; Cu_amine_oxidase_N3.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02728; Cu_amine_oxidN3; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265419};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          105..196
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          229..631
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        391
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         391
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   652 AA;  72627 MW;  76A47E4D7631A4ED CRC64;
     MSETTCEHSL AAAVGHHTLA TPEEVSEARR LLAEAGHFSE TVRLAYIGLI DPAFGLAEDA
     PVDRRFRIQT LDTADNVSRD AIVSVTRGVV ESVRELDTAA TGELPVKDED YGVVEELLAT
     DERWLEALAK RGLDVVKVRV APLSAGVYAD EYPDEKGRRM LRGLAFVQDF PEDSAWAHPV
     EGLLAYVDIT NRKVENVLDF GVVEIPKEHG NYTDPELTGP IRETQKPIVI TQPEGPSFSV
     ENGNHVEWER WSLDVGFDMR DGLVLHNISF DDPNKGRRRI LNRASIAEMV VPYGDPNPVR
     SWQNYFDTGE YLIGQCANSL ELGCDCLGEI TYLSPTIADN DGNPRTIKNG ICMHEEDWSI
     LSKHSDLWTG IDYTRRNRRL VISIFTTVGN YDYGFYWYLY LDGTIEFEAK ATGIVFTSGY
     QGDPTYNSEM ASGLGAPFHQ HQFAARLDFA LDSGVTRVEE EDAVRVPMGP GNPRGNAFTR
     KRTVLSTEKE GVRDADGRIG RSWVISNPES KNRLGEPVAF KLHPMGTPTL LADPESSVAK
     RANVMTHGLW VTRFDETQKY PTGDFANQNP GVEGIAQWIE ADRDIDGQQD VVWHTFGLTH
     YPRIEDWPIM PVDTVGFKLR PEGFFDRSPV LDVPAPVKAH GCCSGGECHC EH
//