ID A0A1P8XP10_9ACTN Unreviewed; 399 AA.
AC A0A1P8XP10;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=BV401_05080 {ECO:0000313|EMBL:AQA09962.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA09962.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL Submitted (JAN-2017) 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 -!- 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|RuleBase:RU000672}.
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DR EMBL; CP019458; AQA09962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8XP10; -.
DR STRING; 75293.BV401_05080; -.
DR KEGG; sauo:BV401_05080; -.
DR OrthoDB; 9772590at2; -.
DR Proteomes; UP000187851; Chromosome.
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; 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 PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000672};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|PIRSR:PIRSR600269-51, ECO:0000256|RuleBase:RU000672}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..399
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012749529"
FT DOMAIN 54..391
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT MOD_RES 178
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 399 AA; 44126 MW; 84A3B6D8FD9CA767 CRC64;
MSSLFRCARV LIAVVGSLAL WVPGPASAAP ARASAAPSCP AAERIDTTLK NGARWQMCWD
IDRNTGAVLS DVIYTPNRST PTRVLKSASL AEVHVPYDSG QPRFYDVSAI GFGDLEQGTL
TRLGAEDCPD GRLRDFRDTP VLCVEEQPRP FAYKSAVEKG VLHGTDLVVF SVSEIGWYDY
ITEWRFSDDG SITPRSGATG SLSPFQFSDA GSGWPTGVGS TRFSENHSHN IFWRLDFDVD
GESKNTVEQY DYPGSGTAAR TTKRTVLSHE TAADLAPARF WRVVNPTAEN TDGHVKSWEI
DNHHSDQYRG PHETEEFTHH DMYFTQYRGC ERLAYGNTAP DCATSVDKYT GGERLTDPVA
WVSVGFHHVP RDEDQDPMPT HWQGFTIVPR DVTATSQLP
//
