ID A0A238XQV5_HALVU Unreviewed; 497 AA.
AC A0A238XQV5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
DE Flags: Fragment;
GN ORFNames=SAMN06264855_12151 {ECO:0000313|EMBL:SNR61327.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR61327.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR61327.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR61327.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|RuleBase:RU000672}.
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DR EMBL; FZNQ01000021; SNR61327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238XQV5; -.
DR OrthoDB; 296432at2157; -.
DR Proteomes; UP000198397; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000198397};
KW TPQ {ECO:0000256|RuleBase:RU000672}.
FT DOMAIN 49..470
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SNR61327.1"
SQ SEQUENCE 497 AA; 56777 MW; 6B5D0FACCB2794E9 CRC64;
IHAWVDLDER EVVKLVDTGP KNTNVVENLR THYYREGKRD LRDDLTPYNV IQPDGPSWNV
DGHTVEWQNW HVRVGFNHRE GLVLYDITYE DEGTERPILR RASYPEVVTA YNDPDPDHDW
KAPFDVGEYG LGRLANSLTE GCDCLGYMHY WDAVLNDGDG NAQVIPNAIC LHEEDYGLLW
KHYDWRVGDH EVRRNRRLVI SFISTIGNYD FAFYWYFYQD GSIESEVRLT GCNATGLLSG
DNRETGYSET IGPGHKSMLH QHVFNCRLDF TIDGETNTVR EVNLNDVPYG PEGYDPTPHA
GVTDQNLNPH GNAAYVERTR LERESDAQRM TDTHAGRYWE IVNENVTNDA TGEPVGYRLM
PKAGTNTAFP MQPGSSNAKR AGFATKHLWV SQYDDAERYP AGEYPNQHPG GVGLPVWTDA
DRSIANEDLV VWYNMCQTHV SVPEDWPILP TKMVSFKLEP AHFFEENPAI DVPPEHAIKD
IDKWKTENQE GMDLEDN
//
