ID A0A0M2HA47_9MICO Unreviewed; 642 AA.
AC A0A0M2HA47;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=RS82_02753 {ECO:0000313|EMBL:KJL41524.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41524.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL41524.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41524.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL41524.1}.
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DR EMBL; JYJA01000037; KJL41524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2HA47; -.
DR PATRIC; fig|69370.6.peg.2798; -.
DR OrthoDB; 9772590at2; -.
DR Proteomes; UP000034098; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000672}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000672,
KW ECO:0000313|EMBL:KJL41524.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW TPQ {ECO:0000256|PIRSR:PIRSR600269-50, ECO:0000256|RuleBase:RU000672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 611..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..423
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 423..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 194
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 194
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 642 AA; 67468 MW; 4FFF92D26B850115 CRC64;
MTMETPPMKR TSLRRLLGAG TAMALLAGGL VLSAPVAASA QTVTEASCSG ESLVSETLES
GSSWQMCWRL DTYRGLVLDK IAYQPRDDAA PILVLDSIAL AQLNVPYDTG ATEYNDVTTY
QVGGRRLQAI EAVDCPVGEV FNAWVDATRG SIPALCIGEE DSGLAYRSNI ARDALYAAQG
TDLVLHTVSR IGWYEYQTEY RFHDDGEISV RLGATGDLSP NDYVNVVNQG WPIAPGQEDF
AVNHYHSAFW RVDFGIDSGA NQVVEKFATT PTGEYGTTGD TGHTAILETQ LTQITNETKT
MGANREAYRV VNPESLNADG HARSYEIIVP RDQAYNLNPE TDFDIAFTSA KSDEVHASHN
LIPSKAGQMV TDYIADGETL EDPVAWVNVG FHHINRDEDQ SPMPIHWQGF TLYPRDFAAQ
NPNIPEGRKW VNGDMRGVPN PNITPTPTAS PTPTPTTEPT GEPTPTATPT TPGNGNGNGN
GNGNGNGNGN GNGNGNGNGA TPAPASVTFG SGEVAPGAAQ TATAAGFTPG ETVSAVLHSD
PVAVGTFVAD SEGVVSAQFV VPSATPAGEH TLVLTGQTSS AVAQGTFTVA SASPAAVFGA
LATTGTDANR WALSGLVLLV AGAGLAGTSW YLRRQQSLKA HA
//
