ID   A0A2T2YC95_9BACT        Unreviewed;       701 AA.
AC   A0A2T2YC95;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=AHMF7605_06095 {ECO:0000313|EMBL:PSR53129.1};
OS   Adhaeribacter arboris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR53129.1, ECO:0000313|Proteomes:UP000240357};
RN   [1] {ECO:0000313|EMBL:PSR53129.1, ECO:0000313|Proteomes:UP000240357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7605 {ECO:0000313|EMBL:PSR53129.1,
RC   ECO:0000313|Proteomes:UP000240357};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL   Submitted (MAR-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|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:PSR53129.1}.
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DR   EMBL; PYFT01000001; PSR53129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2YC95; -.
DR   OrthoDB; 9772590at2; -.
DR   Proteomes; UP000240357; 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; 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   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   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}; Signal {ECO:0000256|SAM:SignalP};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..701
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015728713"
FT   DOMAIN          43..123
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          253..660
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        329
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        408
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         408
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   701 AA;  78900 MW;  A936DE4A8676B59C CRC64;
     MKNLRLLAIA CSASFITVAF SRCSQSGKAE TNASQANNVM LAHPLDPLDS TEIKLVKEIL
     IKNKIFDKEH FFSFIKLNEP SKAEVLSFKP GQPFRREAIA SIYHYKKNIL SEVTLDLKNR
     KVLGIDTLDK MQPVGQFKAD SVALNSTMIK NAEWVSALKK RGISIDSVIH HGNDASDLSM
     GPIGHREKII AAHYKNKKHG RLPIMGLYAF VDLTDHKVLK IVDQGQGFSE PIDVNYFKED
     SAIATIPDTK PLKITQPDGA TFTIKGHEIT WNNWKFRYGI SNREGLIIYQ ASYKDNGKWR
     SVMYRGSMPE MVVNYGSPDI LNASNNYFDV GTYRLAQDKA RPMTPGVDAP ENAVYLTTTL
     HDEQGKIKPF ERAIAVYEEF DGPLWRHNEK GRKSTNLALK YFTTIGNYDY GFKWVFKQDG
     NIDVVTELNG IVHIRGVQRV NDLPGAPDDT YKGNYYGTLV SEHVEAVNHQ HFFVYRMDMD
     VDGPINSVAE MNTVSVLEKE LNPLKSTMVA QMTHLKNEKE AQRSNNIASA RHWKIMNEQV
     QDKWGHHSSY MLMPSPGVKP FAMEGSSLMN RAGFLKNHLW ITPLHEKEIY PAGEYPESKL
     KNAGLPTWTA ANRNIENKDL VMWYVAGVTH IVRPEEWPIM TPHVVKFTLM PNGFFSQNPV
     VRMPKLKTAP KPIASAAGKN LAGGIAYDKS VQCATPVKGI N
//