ID E8N7W2_MICTS Unreviewed; 710 AA.
AC E8N7W2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN OrderedLocusNames=MTES_2618 {ECO:0000313|EMBL:BAJ75582.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ75582.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ75582.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ75582.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012052; BAJ75582.1; -; Genomic_DNA.
DR AlphaFoldDB; E8N7W2; -.
DR STRING; 979556.MTES_2618; -.
DR KEGG; mts:MTES_2618; -.
DR eggNOG; COG3733; Bacteria.
DR HOGENOM; CLU_011500_3_2_11; -.
DR Proteomes; UP000008975; Chromosome.
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.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 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 TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 46..131
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 141..235
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 263..660
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 670..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 419
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 419
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 710 AA; 77283 MW; 5A5F77A8C52D1746 CRC64;
MTGCRGPGAA ASVLLLSALP VPLERDTMTL TDPTSTAFVA PAVPAHPLAS LIPEEITAVH
AIVAGLDGID EATRFAYVGL EEAPKGEVLA WERGESAFPE RRARVQLLNL RTAHSLDLVV
SLASGEVLRS TELDGSDGQL PILDAEFEEV GVIANESTEW VAALAARGLT TADVVLVPLS
AGHYGYENEV GRRVLRTFAF RQDHPADHPW AHPVDGLTAY IDVADRRIIE IVDTPGFTVP
ETHGNFDDPE LQGPPLEGLK PIVITQPEGS SFTVDGEHVT WGEWDLRIGF DTREGLILRQ
LSFAGRPVMY RGSISEMVVP YADPAPNRFW QNYFDTGEYL FGRYTNELEL GCDCVGDITY
VDAVLSDENG MPRTVRNAVC MHEEDFGTLW KHTDIFTGSS EVRRSRRLVI SFFTTVGNYD
YGFYWYLYLD GTIECEAKLT GILFTSGYPG EGYPYASEVA PGLGAPYHQH LFSARLDMTV
DGVANVVNEI DAVRVPISPE NPAGNAFTKK VTPITSEKVS GRVADGAVNR VWQIASTEKT
TERGQATSYV LFPTETPVLL ADDASSIAAR AAFATKNLFV TKYDPDERYA AGDFVNQHPG
GAGIPAFIAG DEPLVGEDLV LWHTFGLTHF PRNEDWPVMP MDYAKFTLKP YNFFERNPVL
NVPAPADTHC APGAHADGHG HGPHADEATG AHGHDHSAHG HDGHGDAHHC
//
