ID A0A0D8CG47_9PROT Unreviewed; 642 AA.
AC A0A0D8CG47;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=UF64_11370 {ECO:0000313|EMBL:KJE35240.1};
OS Thalassospira sp. HJ.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1616823 {ECO:0000313|EMBL:KJE35240.1, ECO:0000313|Proteomes:UP000032356};
RN [1] {ECO:0000313|EMBL:KJE35240.1, ECO:0000313|Proteomes:UP000032356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HJ {ECO:0000313|EMBL:KJE35240.1,
RC ECO:0000313|Proteomes:UP000032356};
RA Kiseleva L., Garushyants S.K., Goryanin I.;
RT "Complete genome of Thalassospira sp. strain HJ.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001138};
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:KJE35240.1}.
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DR EMBL; JYII01000012; KJE35240.1; -; Genomic_DNA.
DR RefSeq; WP_044828662.1; NZ_JYII01000012.1.
DR AlphaFoldDB; A0A0D8CG47; -.
DR STRING; 1616823.UF64_11370; -.
DR PATRIC; fig|1616823.3.peg.546; -.
DR OrthoDB; 9772590at2; -.
DR Proteomes; UP000032356; Unassembled WGS sequence.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
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; IPR015800; Cu_amine_oxidase_N2.
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; PF02727; Cu_amine_oxidN2; 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:UP000032356};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 14..98
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 104..199
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 228..626
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 385
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 385
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 642 AA; 71879 MW; 8E988A2CF6D3E30F CRC64;
MDKCCSSEKV EITHPLQPLT AEEIIKVAEI VRADPPYGEN TLFETIELME PEKDELADFQ
PGDAIARKAR VNVFDATKVS VTKLVLDLEA AKIISAKEMP GKRPMIQLEQ FVEIEEIVCS
DPTFIAACKK RGITDMSMVC VDPWSAGNFG KPGEEGRHLA HIFCWLRKRE NSNFYANPIE
GLNAVVDLLS KEVIRVDDYG GAPIPEAEVN YEADFFEEDE FQPKAKPINV VQPEGVNFKM
DGNKITWRNW ELVIGFNARE SLTLHDIKFN GRPIIHRASI VEMTVPYGSP DNGHYRKNVF
DIGEYGIGKL ANSLTLGCDC LGVIKYLDVT LNTMNGEPWT IENAICIHEE DAGLLWKHMD
FRTERTESRR NAKLVISTIC TVGNYEYALY WYLFLDGMIE FEVKATGIIN TAACLPGEPG
KYAVEVSPGV AGQIHQHILC ARLDMAIDGY GNSPVECNTF AEEPGPENPY GNAFFEKETV
LESELAAARK TNPASQRYWK VVNPNKLGKT GRPVGYKLDA TNCVTPFINP EYPSGKRASF
IENHVWFTAY DPEERFPAGD FMNHSDGRGG LSDFIKKDRA LHNTDLVMWH VFGLHHQVRM
EDFPVQPCVT TGFKLMPMGF FDGNPGINLP PEKNDASCPA KC
//
