ID A0A367AWX9_9ACTN Unreviewed; 652 AA.
AC A0A367AWX9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=DQ237_16470 {ECO:0000313|EMBL:RBY93768.1};
OS Blastococcus sp. TF02-8.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY93768.1, ECO:0000313|Proteomes:UP000252403};
RN [1] {ECO:0000313|EMBL:RBY93768.1, ECO:0000313|Proteomes:UP000252403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-8 {ECO:0000313|EMBL:RBY93768.1,
RC ECO:0000313|Proteomes:UP000252403};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-8.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RBY93768.1}.
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DR EMBL; QOHK01000009; RBY93768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367AWX9; -.
DR OrthoDB; 9772590at2; -.
DR Proteomes; UP000252403; 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:SF18; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER 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 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:UP000252403};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 25..86
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 122..216
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 246..642
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 401
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 401
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 652 AA; 73125 MW; B1FB99A4C01BF7B0 CRC64;
MTDPAPSCHS SVGSAGTSAP PGTPHPLDPL SAEEFRAAAS ILRRDRGVDE RWRFAAIELR
EPAKDVVRGF RPGDPIRREA RVTAWSRDEG IPYKAVVSLP DGQDAEGGVV SWEAVPGQQA
NMTVDEWHEA HEALIRHPDV VAALAKRGIT DLDLVLIDTW AYGHSLIPQG FQDRRVGWTD
VWRRAAPDAN PYANPVMGLH FVVDLNSMEL LQIEDTAPPA EAPVMGEYVP SLVPGLQQRT
DVKALEIMQP EGVSFALDGH ELRWQKWTMR LGFNYREGLV IHRLEYDGRP VAHRMSFAEM
VVPYRDPSPD HHRRTAFDAG EWGLGFMTTS LKLGCDCLGD ITYVDAVLHD TRGEPYTIEN
AICLHEEDDG VLWKHVDEQA GSEVRRSRRM VVSFHATVAN YEYLTYWRFY QDGTIQCEVR
ATGIMVTSAF EGEAPPYGTV VDERTYAPIH QHFIVARLDM EVDGPENTVV VTESEALPVS
AENPHGLAVV TRSRPVESEA EGRLDVDFAT QRSFKVVNRT KPNRLGTAPG FKLYPSSALP
SMAHPDAPFR QRAQVIDHPV WVSRFDEEER WPAGEFCNQS RRDEGLPEWQ KADRPLVDTD
VVLWHVFGIH HVPRPEDWPV MPVDVVSFEL KPVGFFDRNP ALDVPPAPGR CH
//
