ID A0A0M2HJY9_9MICO Unreviewed; 660 AA.
AC A0A0M2HJY9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=RS84_03718 {ECO:0000313|EMBL:KJL47070.1};
OS Microbacterium hydrocarbonoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL47070.1, ECO:0000313|Proteomes:UP000033900};
RN [1] {ECO:0000313|EMBL:KJL47070.1, ECO:0000313|Proteomes:UP000033900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA35 {ECO:0000313|EMBL:KJL47070.1,
RC ECO:0000313|Proteomes:UP000033900};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL47070.1}.
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DR EMBL; JYJB01000010; KJL47070.1; -; Genomic_DNA.
DR RefSeq; WP_045259145.1; NZ_JYJB01000010.1.
DR AlphaFoldDB; A0A0M2HJY9; -.
DR STRING; 273678.RS84_03718; -.
DR PATRIC; fig|273678.4.peg.3711; -.
DR Proteomes; UP000033900; 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; PS01165; COPPER_AMINE_OXID_2; 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:UP000033900};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 112..207
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 233..631
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 389
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 389
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 660 AA; 72055 MW; 39B2EA9E394ED69E CRC64;
MSHQPVTIEK IAAPHPLDPL TGAEIAAARA VLEAAGLMGE TVRVPMLLPD EPTKAELAAW
KPDAPIDRRV DATLLDTATG VATEVIVSVT RGEVVSATRV PNDAPPYGQP QYLFEEYERA
EAIAKASPEW QAAMTRRGLA EHMDLAFCGP LAPGYTGRAD EVGRRVIRSL TFLRYDEHDS
PWAHPVEGLI VHIDLTSNSV IRIEDVGDVP VPAGHGNYYP EAQGEARTSL KPIEITQPHG
PSFAVTGSLV EWENWSMRVS FNAREGLVLH DVTFDGRSVL SRASVPEMVV PYGDTAPGRF
WISYFDAGEY LLGKNANHLE LGCDCLGVIR YLDGYVADDH GHPVRIPNVI CMHEEDYGIL
WKHTNLEGRS DVRRSRRFVV SYFSTIGNYD YGFYWHFYLD GSIEVTAKAT GIVFVGAGEP
GVPQKHATEL VPGVFAPVHQ HLFSARLDVA IDGEDNRLVE IDAQRVPMGP ENPFGNAFTW
SETPLSSEKQ AQREADTSVA RVWEVQSASR TNAVGRPTAY HLIPEPTALL MADPASSVAA
RAAFATKHLW ATQHEQGQIW PAGRYPNAHQ GGSGLPEYSA GDRSLDGEDI VLWHTFGLTH
FPRLEDWPIM PVDYAGFWLK PYGFLDQNPA MDVPESSQAH GSAAADAGCC GGGAGCTCAH
//
