ID A0A418KJD4_9ACTN Unreviewed; 482 AA.
AC A0A418KJD4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=DY240_24685 {ECO:0000313|EMBL:RIQ14462.1};
OS Jiangella rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Jiangella.
OX NCBI_TaxID=2293569 {ECO:0000313|EMBL:RIQ14462.1, ECO:0000313|Proteomes:UP000284057};
RN [1] {ECO:0000313|EMBL:RIQ14462.1, ECO:0000313|Proteomes:UP000284057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY265 {ECO:0000313|EMBL:RIQ14462.1,
RC ECO:0000313|Proteomes:UP000284057};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (SEP-2018) 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}.
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:RIQ14462.1}.
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DR EMBL; QUAL01000347; RIQ14462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418KJD4; -.
DR OrthoDB; 9772590at2; -.
DR Proteomes; UP000284057; 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 Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|PIRSR:PIRSR600269-50, ECO:0000256|RuleBase:RU000672}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..482
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019558217"
FT DOMAIN 48..409
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 409..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 180
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 180
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 482 AA; 53231 MW; 43FA8ADCB9F11A27 CRC64;
MRVPKLVLAA ALAASSLAGF TSTASAASVT ELSCSGPSLV KETLRSGSGW EMCWRIDSYR
GLVVDKVAFT PRDEGRPVMV LDSIGLAQLN VPYDTGMTEY NDVTTYQVGG RRMQDQTAID
CPAGEIRSSY LTETRPLAPV LCVSEQEAGL AYRSNVANDA LYAAQGTHLV LHTVSRIGWY
EYQTEYRFHD DGEITVRLGA TGDLSPNDYV DAVNFGWPIA EGQEDFAVNH YHSAFWRVAF
DIDSATRQRV EKIDSDFTGE YGTTGDTGKT PIIETEISPV NREQKLILEN REAYRVVNPD
SLNADGHPRS YEIVMDRAQA YALNPETDYD LAFTEPKSDE IFASYNLLPS KPNASVTQYV
ADRERLRKPV AWVNVGFHHI VRDEDQSPMP IHWQGFTLYP RDFTAQNPNI PEGRKWVNGD
MRGVPNPNIT PTPTPTPTAT PTVTPTPSAS PTTTPTPSAS PTTTRPRPTP VPRPTGRPTG
WR
//
