ID A1R2C3_PAEAT Unreviewed; 656 AA.
AC A1R2C3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN OrderedLocusNames=AAur_0579 {ECO:0000313|EMBL:ABM10002.1};
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paenarthrobacter.
OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM10002.1, ECO:0000313|Proteomes:UP000000637};
RN [1] {ECO:0000313|EMBL:ABM10002.1, ECO:0000313|Proteomes:UP000000637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:ABM10002.1,
RC ECO:0000313|Proteomes:UP000000637};
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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}.
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DR EMBL; CP000474; ABM10002.1; -; Genomic_DNA.
DR RefSeq; WP_011773333.1; NC_008711.1.
DR AlphaFoldDB; A1R2C3; -.
DR STRING; 290340.AAur_0579; -.
DR KEGG; aau:AAur_0579; -.
DR eggNOG; COG3733; Bacteria.
DR HOGENOM; CLU_011500_3_2_11; -.
DR OrthoDB; 9772590at2; -.
DR BRENDA; 1.4.3.21; 441.
DR Proteomes; UP000000637; Chromosome.
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; 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; 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; 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 TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 111..203
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 232..634
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 637..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 393
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 393
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 656 AA; 72378 MW; DFCD6FDA0C81C89E CRC64;
MTLQTTPLAA TTQAPLGQHP LEQLSAHEIH QARRILADAG LVAETTRFAY LGLIEPPKAV
FQADAADAPR LVRAMLWDAA QSRSLDVRLS LATGLVLDQR ELNPEIDGQL PVLLEEFGII
EDILAVDPQW NAALASRGLT PAQVRVAPLS AGVFEYGNEE GKRLLRGLGF RQDHPADHPW
AHPIDGLVAF VDIENRRVNH LIDDGPVPVP EVNGNYTDPT IHGELRTDLK PIEITQPEGP
SFTLEGNHLS WAGWDLRVGF DAREGLVLHQ LHHSHQGRRR PVVHRASISE MVVPYGDPSP
YRSWQNYFDS GEYLVGRDAN SLKLGCDCLG DITYMSPVVA DDFGNPRVIE NGICIHEEDA
GILWKHTDEW AGSNEVRRNR RLVVSFFTTV GNYDYGFYWY LYLDGTIEFE AKATGIVFTA
ALPDKDYAYA SEIAPGLGAP YHQHLFSARL DMMVDGGTNR VEELDLVRLP KGPGNPHGNA
FTQKRTVLTR ESEAVRDADG TKGRVWHISN PDSLNHLGHP VGYTLYPEGN PTLAMADDSS
IASRAAFAKH HLWVTQHAED ELYAAGDFVN QHPGGAGLPS YVAQDRDIDG QDLVVWHSFG
LTHFPRPEDW PIMPVDTTGF TLKPHGFFDQ NPTLNVPSSS TGHCAPAEQN TGTCGH
//
