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Database: UniProt
Entry: A0A225NJC1_9RHOB
LinkDB: A0A225NJC1_9RHOB
Original site: A0A225NJC1_9RHOB 
ID   A0A225NJC1_9RHOB        Unreviewed;       639 AA.
AC   A0A225NJC1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=ATO3_17045 {ECO:0000313|EMBL:OWU72261.1};
OS   Marinibacterium profundimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Marinibacterium.
OX   NCBI_TaxID=1679460 {ECO:0000313|EMBL:OWU72261.1, ECO:0000313|Proteomes:UP000215377};
RN   [1] {ECO:0000313|EMBL:OWU72261.1, ECO:0000313|Proteomes:UP000215377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-22F33 {ECO:0000313|EMBL:OWU72261.1,
RC   ECO:0000313|Proteomes:UP000215377};
RA   Lai Q., Li G., Shao Z.;
RT   "Oceanicola sp. 22II1-22F33 Genome Sequencing.";
RL   Submitted (APR-2013) 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:OWU72261.1}.
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DR   EMBL; AQQR01000007; OWU72261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225NJC1; -.
DR   OrthoDB; 9772590at2; -.
DR   Proteomes; UP000215377; 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:UP000215377};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          15..79
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          105..205
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          228..624
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        384
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         384
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   639 AA;  72110 MW;  FDDE7E351D9C4844 CRC64;
     MNIADTTAFN TKVSHPLDPL SASEIEKAAR LVRGHMGGAD LRFETIELKE PEKGSVRAWQ
     QGGETPKRTA RVNTFRPGKI GVWRFIVSLT DGAISREEHF PEARPMIMLE EFMQIEDTVK
     AHPDFIEACR KRGIEDLDLV CVDPWSAGNF DVEGEEGKHL AHTFCWVRMR PDDNLYAHPI
     EGLNPVVDIK KMEVIRVDDY GAVPVPEMEV NYDAQFIDEM REDLRPIDVV QPEGVTFTME
     GRTIKWHDWS ILIGFNGREG LTLHDIRYAD RPVLYRASIA EMVVPYGAPD AQHARKNVFD
     IGEYGLGKLA NSLELGCDCL GVIHYLDAEI PGIEGTSETI RNAICIHEED TGILWKHWDF
     RTDKTEVRRG RRLVISSIST VGNYEYASYW YFYLDGKIEF EMKATGIINT VGKTPETDMR
     FGTEVAPGVI GQIHQHLFVA RLDLSIDGDE NQVFECNTQA LPMGPDNPYG NAFFVEETKL
     DKECGRTIAP EKQRYWKFAS SDKTNYMGKP TAYKLEPSHA VTPFNNPEGP SGARMPFIYN
     HLWLSEYHAD ERFPAGDFMN HSDGSQGVHK AAERGNSIDG KDVVAWHVFG LHHNVRLEDF
     PVQPVISCGF MLMPNGFFDM NPCLDLPAEK NEASCCAAE
//
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